Acta crystallographica. Section D, Biological crystallography最新文献_第4页

Combining phase information in reciprocal space for molecular replacement with partial models. 结合互易空间相信息与部分模型进行分子置换。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-09-01 Epub Date: 2015-08-25 DOI: 10.1107/S1399004715013127

Claudia Millán, Massimo Sammito, Irene Garcia-Ferrer, Theodoros Goulas, George M Sheldrick, Isabel Usón

{"title":"Combining phase information in reciprocal space for molecular replacement with partial models.","authors":"Claudia Millán, Massimo Sammito, Irene Garcia-Ferrer, Theodoros Goulas, George M Sheldrick, Isabel Usón","doi":"10.1107/S1399004715013127","DOIUrl":"https://doi.org/10.1107/S1399004715013127","url":null,"abstract":"ARCIMBOLDO allows ab initio phasing of macromolecular structures below atomic resolution by exploiting the location of small model fragments combined with density modification in a multisolution frame. The model fragments can be either secondary-structure elements predicted from the sequence or tertiary-structure fragments. The latter can be derived from libraries of typical local folds or from related structures, such as a low-homology model that is unsuccessful in molecular replacement. In all ARCIMBOLDO applications, fragments are searched for sequentially. Correct partial solutions obtained after each fragment-search stage but lacking the necessary phasing power can, if combined, succeed. Here, an analysis is presented of the clustering of partial solutions in reciprocal space and of its application to a set of different cases. In practice, the task of combining model fragments from an ARCIMBOLDO run requires their referral to a common origin and is complicated by the presence of correct and incorrect solutions as well as by their not being independent. The F-weighted mean phase difference has been used as a figure of merit. Clustering perfect, non-overlapping fragments dismembered from test structures in polar and nonpolar space groups shows that density modification before determining the relative origin shift enhances its discrimination. In the case of nonpolar space groups, clustering of ARCIMBOLDO solutions from secondary-structure models is feasible. The use of partially overlapping search fragments provides a more favourable circumstance and was assessed on a test case. Applying the devised strategy, a previously unknown structure was solved from clustered correct partial solutions. ","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 9","pages":"1931-45"},"PeriodicalIF":0.0,"publicationDate":"2015-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715013127","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33965228","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 17

The catalytic mechanism and unique low pH optimum of Caldicellulosiruptor bescii family 3 pectate lyase. 贝氏钙纤维素裂解酶家族3果胶裂解酶的催化机理及独特的低pH条件。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-09-01 Epub Date: 2015-08-25 DOI: 10.1107/S1399004715013760

Markus Alahuhta, Larry E Taylor, Roman Brunecky, Deanne W Sammond, William Michener, Michael W W Adams, Michael E Himmel, Yannick J Bomble, Vladimir Lunin

{"title":"The catalytic mechanism and unique low pH optimum of Caldicellulosiruptor bescii family 3 pectate lyase.","authors":"Markus Alahuhta, Larry E Taylor, Roman Brunecky, Deanne W Sammond, William Michener, Michael W W Adams, Michael E Himmel, Yannick J Bomble, Vladimir Lunin","doi":"10.1107/S1399004715013760","DOIUrl":"10.1107/S1399004715013760","url":null,"abstract":"The unique active site of the Caldicellulosiruptor bescii family 3 pectate lyase (PL3) enzyme has been thoroughly characterized using a series of point mutations, X-ray crystallography, pK(a) calculations and biochemical assays. The X-ray structures of seven PL3 active-site mutants, five of them in complex with intact trigalacturonic acid, were solved and characterized structurally, biochemically and computationally. The results confirmed that Lys108 is the catalytic base, but there is no clear candidate for the catalytic acid. However, the reaction mechanism can also be explained by an antiperiplanar trans-elimination reaction, in which Lys108 abstracts a proton from the C5 atom without the help of simultaneous proton donation by an acidic residue. An acidified water molecule completes the anti β-elimination reaction by protonating the O4 atom of the substrate. Both the C5 hydrogen and C4 hydroxyl groups of the substrate must be orientated in axial configurations, as for galacturonic acid, for this to be possible. The wild-type C. bescii PL3 displays a pH optimum that is lower than that of Bacillus subtilis PL1 according to activity measurements, indicating that C. bescii PL3 has acquired a lower pH optimum by utilizing lysine instead of arginine as the catalytic base, as well as by lowering the pK(a) of the catalytic base in a unique active-site environment.","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 9","pages":"1946-54"},"PeriodicalIF":0.0,"publicationDate":"2015-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715013760","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33965229","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 11

Crystallography and chemistry should always go together: a cautionary tale of protein complexes with cisplatin and carboplatin. 晶体学和化学应该总是结合在一起:顺铂和卡铂的蛋白质复合物的警示故事。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-09-01 Epub Date: 2015-08-28 DOI: 10.1107/S139900471500629X

Ivan Shabalin, Zbigniew Dauter, Mariusz Jaskolski, Wladek Minor, Alexander Wlodawer

{"title":"Crystallography and chemistry should always go together: a cautionary tale of protein complexes with cisplatin and carboplatin.","authors":"Ivan Shabalin, Zbigniew Dauter, Mariusz Jaskolski, Wladek Minor, Alexander Wlodawer","doi":"10.1107/S139900471500629X","DOIUrl":"10.1107/S139900471500629X","url":null,"abstract":"The anticancer activity of platinum-containing drugs such as cisplatin and carboplatin is considered to primarily arise from their interactions with nucleic acids; nevertheless, these drugs, or the products of their hydrolysis, also bind to proteins, potentially leading to the known side effects of the treatments. Here, over 40 crystal structures deposited in the Protein Data Bank (PDB) of cisplatin and carboplatin complexes of several proteins were analysed. Significant problems of either a crystallographic or a chemical nature were found in most of the presented atomic models and they could be traced to less or more serious deficiencies in the data-collection and refinement procedures. The re-evaluation of these data and models was possible thanks to their mandatory or voluntary deposition in publicly available databases, emphasizing the point that the availability of such data is critical for making structural science reproducible. Based on this analysis of a selected group of macromolecular structures, the importance of deposition of raw diffraction data is stressed and a procedure for depositing, tracking and using re-refined crystallographic models is suggested. ","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 9","pages":"1965-79"},"PeriodicalIF":0.0,"publicationDate":"2015-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S139900471500629X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33967365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 48

Insights into stabilizing interactions in the distorted domain-swapped dimer of Salmonella typhimurium survival protein. 鼠伤寒沙门氏菌存活蛋白扭曲结构域交换二聚体中稳定相互作用的见解。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-09-01 Epub Date: 2015-08-25 DOI: 10.1107/S1399004715011992

Yamuna Kalyani Mathiharan, H S Savithri, M R N Murthy

{"title":"Insights into stabilizing interactions in the distorted domain-swapped dimer of Salmonella typhimurium survival protein.","authors":"Yamuna Kalyani Mathiharan, H S Savithri, M R N Murthy","doi":"10.1107/S1399004715011992","DOIUrl":"https://doi.org/10.1107/S1399004715011992","url":null,"abstract":"The survival protein SurE from Salmonella typhimurium (StSurE) is a dimeric protein that functions as a phosphatase. SurE dimers are formed by the swapping of a loop with a pair of β-strands and a C-terminal helix between two protomers. In a previous study, the Asp230 and His234 residues were mutated to Ala to abolish a hydrogen bond that was thought to be crucial for C-terminal helix swapping. These mutations led to functionally inactive and distorted dimers in which the two protomers were related by a rotation of 167°. New salt bridges involving Glu112 were observed in the dimeric interface of the H234A and D230A/H234A mutants. To explore the role of these salt bridges in the stability of the distorted structure, E112A, E112A/D230A, E112A/H234A, E112A/D230A/H234A, R179L/H180A/H234A and E112A/R179L/H180A/H234A mutants were constructed. X-ray crystal structures of the E112A, E112A/H234A and E112A/D230A mutants could be determined. The dimeric structures of the E112A and E112A/H234A mutants were similar to that of native SurE, while the E112A/D230A mutant had a residual rotation of 11° between the B chains upon superposition of the A chains of the mutant and native dimers. The native dimeric structure was nearly restored in the E112A/H234A mutant, suggesting that the new salt bridge observed in the H234A and D230A/H234A mutants was indeed responsible for the stability of their distorted structures. Catalytic activity was also restored in these mutants, implying that appropriate dimeric organization is necessary for the activity of SurE. ","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 9","pages":"1812-23"},"PeriodicalIF":0.0,"publicationDate":"2015-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715011992","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34034508","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 4

Structure of the 34 kDa F-actin-bundling protein ABP34 from Dictyostelium discoideum. 盘状盘齿龙f -肌动蛋白结合蛋白ABP34的结构。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-09-01 Epub Date: 2015-08-25 DOI: 10.1107/S139900471501264X

Min-Kyu Kim, Ji-Hye Kim, Ji-Sun Kim, Sa-Ouk Kang

{"title":"Structure of the 34 kDa F-actin-bundling protein ABP34 from Dictyostelium discoideum.","authors":"Min-Kyu Kim, Ji-Hye Kim, Ji-Sun Kim, Sa-Ouk Kang","doi":"10.1107/S139900471501264X","DOIUrl":"https://doi.org/10.1107/S139900471501264X","url":null,"abstract":"The crystal structure of the 34 kDa F-actin-bundling protein ABP34 from Dictyostelium discoideum was solved by Ca(2+)/S-SAD phasing and refined at 1.89 Å resolution. ABP34 is a calcium-regulated actin-binding protein that cross-links actin filaments into bundles. Its in vitro F-actin-binding and F-actin-bundling activities were confirmed by a co-sedimentation assay and transmission electron microscopy. The co-localization of ABP34 with actin in cells was also verified. ABP34 adopts a two-domain structure with an EF-hand-containing N-domain and an actin-binding C-domain, but has no reported overall structural homologues. The EF-hand is occupied by a calcium ion with a pentagonal bipyramidal coordination as in the canonical EF-hand. The C-domain structure resembles a three-helical bundle and superposes well onto the rod-shaped helical structures of some cytoskeletal proteins. Residues 216-244 in the C-domain form part of the strongest actin-binding sites (193-254) and exhibit a conserved sequence with the actin-binding region of α-actinin and ABP120. Furthermore, the second helical region of the C-domain is kinked by a proline break, offering a convex surface towards the solvent area which is implicated in actin binding. The F-actin-binding model suggests that ABP34 binds to the side of the actin filament and residues 216-244 fit into a pocket between actin subdomains -1 and -2 through hydrophobic interactions. These studies provide insights into the calcium coordination in the EF-hand and F-actin-binding site in the C-domain of ABP34, which are associated through interdomain interactions. ","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 9","pages":"1835-49"},"PeriodicalIF":0.0,"publicationDate":"2015-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S139900471501264X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34034510","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 5

Advances in molecular-replacement procedures: the REVAN pipeline. 分子替代程序的进展:REVAN管道。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-09-01 Epub Date: 2015-08-28 DOI: 10.1107/S1399004715012730

Benedetta Carrozzini, Giovanni Luca Cascarano, Carmelo Giacovazzo, Annamaria Mazzone

{"title":"Advances in molecular-replacement procedures: the REVAN pipeline.","authors":"Benedetta Carrozzini, Giovanni Luca Cascarano, Carmelo Giacovazzo, Annamaria Mazzone","doi":"10.1107/S1399004715012730","DOIUrl":"https://doi.org/10.1107/S1399004715012730","url":null,"abstract":"The REVAN pipeline aiming at the solution of protein structures via molecular replacement (MR) has been assembled. It is the successor to REVA, a pipeline that is particularly efficient when the sequence identity (SI) between the target and the model is greater than 0.30. The REVAN and REVA procedures coincide when the SI is >0.30, but differ substantially in worse conditions. To treat these cases, REVAN combines a variety of programs and algorithms (REMO09, REFMAC, DM, DSR, VLD, free lunch, Coot, Buccaneer and phenix.autobuild). The MR model, suitably rotated and positioned, is first refined by a standard REFMAC refinement procedure, and the corresponding electron density is then submitted to cycles of DM-VLD-REFMAC. The next REFMAC applications exploit the better electron densities obtained at the end of the VLD-EDM sections (a procedure called vector refinement). In order to make the model more similar to the target, the model is submitted to mutations, in which Coot plays a basic role, and it is then cyclically resubmitted to REFMAC-EDM-VLD cycles. The phases thus obtained are submitted to free lunch and allow most of the test structures studied by DiMaio et al. [(2011), Nature (London), 473, 540-543] to be solved without using energy-guided programs. ","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 9","pages":"1856-63"},"PeriodicalIF":0.0,"publicationDate":"2015-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715012730","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34034512","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 7

From deep TLS validation to ensembles of atomic models built from elemental motions. 从深度TLS验证到由元素运动构建的原子模型集成。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-08-01 Epub Date: 2015-07-28 DOI: 10.1107/S1399004715011426

Alexandre Urzhumtsev, Pavel V Afonine, Andrew H Van Benschoten, James S Fraser, Paul D Adams

{"title":"From deep TLS validation to ensembles of atomic models built from elemental motions.","authors":"Alexandre Urzhumtsev, Pavel V Afonine, Andrew H Van Benschoten, James S Fraser, Paul D Adams","doi":"10.1107/S1399004715011426","DOIUrl":"10.1107/S1399004715011426","url":null,"abstract":"The translation-libration-screw model first introduced by Cruickshank, Schomaker and Trueblood describes the concerted motions of atomic groups. Using TLS models can improve the agreement between calculated and experimental diffraction data. Because the T, L and S matrices describe a combination of atomic vibrations and librations, TLS models can also potentially shed light on molecular mechanisms involving correlated motions. However, this use of TLS models in mechanistic studies is hampered by the difficulties in translating the results of refinement into molecular movement or a structural ensemble. To convert the matrices into a constituent molecular movement, the matrix elements must satisfy several conditions. Refining the T, L and S matrix elements as independent parameters without taking these conditions into account may result in matrices that do not represent concerted molecular movements. Here, a mathematical framework and the computational tools to analyze TLS matrices, resulting in either explicit decomposition into descriptions of the underlying motions or a report of broken conditions, are described. The description of valid underlying motions can then be output as a structural ensemble. All methods are implemented as part of the PHENIX project. ","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 8","pages":"1668-83"},"PeriodicalIF":0.0,"publicationDate":"2015-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4528800/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33899166","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 15

Fully automatic characterization and data collection from crystals of biological macromolecules. 生物大分子晶体的全自动表征和数据采集。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-08-01 Epub Date: 2015-07-31 DOI: 10.1107/S1399004715011918

Olof Svensson, Stéphanie Malbet-Monaco, Alexander Popov, Didier Nurizzo, Matthew W Bowler

{"title":"Fully automatic characterization and data collection from crystals of biological macromolecules.","authors":"Olof Svensson, Stéphanie Malbet-Monaco, Alexander Popov, Didier Nurizzo, Matthew W Bowler","doi":"10.1107/S1399004715011918","DOIUrl":"10.1107/S1399004715011918","url":null,"abstract":"Considerable effort is dedicated to evaluating macromolecular crystals at synchrotron sources, even for well established and robust systems. Much of this work is repetitive, and the time spent could be better invested in the interpretation of the results. In order to decrease the need for manual intervention in the most repetitive steps of structural biology projects, initial screening and data collection, a fully automatic system has been developed to mount, locate, centre to the optimal diffraction volume, characterize and, if possible, collect data from multiple cryocooled crystals. Using the capabilities of pixel-array detectors, the system is as fast as a human operator, taking an average of 6 min per sample depending on the sample size and the level of characterization required. Using a fast X-ray-based routine, samples are located and centred systematically at the position of highest diffraction signal and important parameters for sample characterization, such as flux, beam size and crystal volume, are automatically taken into account, ensuring the calculation of optimal data-collection strategies. The system is now in operation at the new ESRF beamline MASSIF-1 and has been used by both industrial and academic users for many different sample types, including crystals of less than 20 µm in the smallest dimension. To date, over 8000 samples have been evaluated on MASSIF-1 without any human intervention.","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 8","pages":"1757-67"},"PeriodicalIF":0.0,"publicationDate":"2015-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4528805/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33900726","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structural and adhesive properties of the long polar fimbriae protein LpfD from adherent-invasive Escherichia coli. 粘附性侵袭型大肠杆菌长极性菌毛蛋白LpfD的结构与粘附特性。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-08-01 Epub Date: 2015-07-28 DOI: 10.1107/S1399004715009803

Fanny Coppens, Jegan Iyyathurai, Ségolène Ruer, Antonella Fioravanti, Joemar Taganna, Lars Vereecke, Henri De Greve, Han Remaut

{"title":"Structural and adhesive properties of the long polar fimbriae protein LpfD from adherent-invasive Escherichia coli.","authors":"Fanny Coppens, Jegan Iyyathurai, Ségolène Ruer, Antonella Fioravanti, Joemar Taganna, Lars Vereecke, Henri De Greve, Han Remaut","doi":"10.1107/S1399004715009803","DOIUrl":"https://doi.org/10.1107/S1399004715009803","url":null,"abstract":"Crohn's disease (CD) is an inflammatory bowel disease characterized by an exaggerated immune response to commensal microbiota in the intestines of patients. Metagenomic studies have identified specific bacterial species and strains with increased prevalence in CD patients, amongst which is the adherent-invasive Escherichia coli (AIEC) strain LF82. AIEC strains express long polar fimbriae (LPF), which are known to target Peyer's patches in a mouse CD model. Here, the recombinant production of a soluble, self-complemented construct of the LpfD protein of E. coli LF82 is reported and it is demonstrated that it forms the adhesive tip subunit of LPF. The LpfD crystal reveals an N-terminal adhesin domain and a C-terminal pilin domain that connects the adhesin to the minor pilus subunit LpfE. Surface topology and sequence conservation in the adhesin domain hint at a putative receptor-binding pocket as found in the Klebsiella pneumoniae MrkD and E. coli F17-G (GafD) adhesins. Immunohistostaining of murine intestinal tissue sections revealed that LpfD specifically binds to the intestinal mucosa and submucosa. LpfD binding was found to be resistant to treatment with O- or N-glycosidases, but was lost in collagenase-treated tissue sections, indicating the possible involvement of an intestinal matrix-associated protein as the LpfD receptor. LpfD strongly adhered to isolated fibronectin in an in vitro assay, and showed lower levels of binding to collagen V and laminin and no binding to collagens I, III and IV. ","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 8","pages":"1615-26"},"PeriodicalIF":0.0,"publicationDate":"2015-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715009803","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33967497","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 9

The quaternary structure of the eukaryotic DNA replication proteins Sld7 and Sld3. 真核DNA复制蛋白Sld7和Sld3的四级结构。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-08-01 Epub Date: 2015-07-28 DOI: 10.1107/S1399004715010457

Hiroshi Itou, Yasuo Shirakihara, Hiroyuki Araki

{"title":"The quaternary structure of the eukaryotic DNA replication proteins Sld7 and Sld3.","authors":"Hiroshi Itou, Yasuo Shirakihara, Hiroyuki Araki","doi":"10.1107/S1399004715010457","DOIUrl":"https://doi.org/10.1107/S1399004715010457","url":null,"abstract":"The initiation of eukaryotic chromosomal DNA replication requires the formation of an active replicative helicase at the replication origins of chromosomes. Yeast Sld3 and its metazoan counterpart treslin are the hub proteins mediating protein associations critical for formation of the helicase. The Sld7 protein interacts with Sld3, and the complex formed is thought to regulate the function of Sld3. Although Sld7 is a non-essential DNA replication protein that is found in only a limited range of yeasts, its depletion slowed the growth of cells and caused a delay in the S phase. Recently, the Mdm2-binding protein was found to bind to treslin in humans, and its depletion causes defects in cells similar to the depletion of Sld7 in yeast, suggesting their functional relatedness and importance during the initiation step of DNA replication. Here, the crystal structure of Sld7 in complex with Sld3 is presented. Sld7 comprises two structural domains. The N-terminal domain of Sld7 binds to Sld3, and the C-terminal domains connect two Sld7 molecules in an antiparallel manner. The quaternary structure of the Sld3-Sld7 complex shown from the crystal structures appears to be suitable to activate two helicase molecules loaded onto replication origins in a head-to-head manner. ","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 8","pages":"1649-56"},"PeriodicalIF":0.0,"publicationDate":"2015-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33967500","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 31