Acta Crystallographica Section D: Biological Crystallography最新文献_第4页

The structure of the GemC1 coiled coil and its interaction with the Geminin family of coiled-coil proteins. GemC1 螺旋线圈的结构及其与螺旋线圈蛋白 Geminin 家族的相互作用。

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2015-11-01 Epub Date: 2015-10-31 DOI: 10.1107/S1399004715016892

Christophe Caillat, Alexander Fish, Dafni Eleftheria Pefani, Stavros Taraviras, Zoi Lygerou, Anastassis Perrakis

{"title":"The structure of the GemC1 coiled coil and its interaction with the Geminin family of coiled-coil proteins.","authors":"Christophe Caillat, Alexander Fish, Dafni Eleftheria Pefani, Stavros Taraviras, Zoi Lygerou, Anastassis Perrakis","doi":"10.1107/S1399004715016892","DOIUrl":"10.1107/S1399004715016892","url":null,"abstract":"GemC1, together with Idas and Geminin, an important regulator of DNA-replication licensing and differentiation decisions, constitute a superfamily sharing a homologous central coiled-coil domain. To better understand this family of proteins, the crystal structure of a GemC1 coiled-coil domain variant engineered for better solubility was determined to 2.2 Å resolution. GemC1 shows a less typical coiled coil compared with the Geminin homodimer and the Geminin-Idas heterodimer structures. It is also shown that both in vitro and in cells GemC1 interacts with Geminin through its coiled-coil domain, forming a heterodimer that is more stable that the GemC1 homodimer. Comparative analysis of the thermal stability of all of the possible superfamily complexes, using circular dichroism to follow the unfolding of the entire helix of the coiled coil, or intrinsic tryptophan fluorescence of a unique conserved N-terminal tryptophan, shows that the unfolding of the coiled coil is likely to take place from the C-terminus towards the N-terminus. It is also shown that homodimers show a single-state unfolding, while heterodimers show a two-state unfolding, suggesting that the dimer first falls apart and the helices then unfold according to the stability of each protein. The findings argue that Geminin-family members form homodimers and heterodimers between them, and this ability is likely to be important for modulating their function in cycling and differentiating cells.","PeriodicalId":6895,"journal":{"name":"Acta Crystallographica Section D: Biological Crystallography","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2015-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4631479/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"61948454","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole. 酵母过氧化物酶体Δ(3)，Δ(2)-烯酰辅酶a异构酶与酰基辅酶a底物类似物络合的结构:氢键网络对催化碱和氧阴离子孔反应性的重要性。

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2015-11-01 DOI: 10.1107/S139900471501559X

G. Onwukwe, M. K. Koski, P. Pihko, W. Schmitz, Rik K. Wierenga

{"title":"Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks for the reactivity of the catalytic base and the oxyanion hole.","authors":"G. Onwukwe, M. K. Koski, P. Pihko, W. Schmitz, Rik K. Wierenga","doi":"10.1107/S139900471501559X","DOIUrl":"https://doi.org/10.1107/S139900471501559X","url":null,"abstract":"Δ(3),Δ(2)-Enoyl-CoA isomerases (ECIs) catalyze the shift of a double bond from 3Z- or 3E-enoyl-CoA to 2E-enoyl-CoA. ECIs are members of the crotonase superfamily. The crotonase framework is used by many enzymes to catalyze a wide range of reactions on acyl-CoA thioesters. The thioester O atom is bound in a conserved oxyanion hole. Here, the mode of binding of acyl-CoA substrate analogues to peroxisomal Saccharomyces cerevisiae ECI (ScECI2) is described. The best defined part of the bound acyl-CoA molecules is the 3',5'-diphosphate-adenosine moiety, which interacts with residues of loop 1 and loop 2, whereas the pantetheine part is the least well defined. The catalytic base, Glu158, is hydrogen-bonded to the Asn101 side chain and is further hydrogen-bonded to the side chain of Arg100 in the apo structure. Arg100 is completely buried in the apo structure and a conformational change of the Arg100 side chain appears to be important for substrate binding and catalysis. The oxyanion hole is formed by the NH groups of Ala70 (loop 2) and Leu126 (helix 3). The O atoms of the corresponding peptide units, Gly69 O and Gly125 O, are both part of extensive hydrogen-bond networks. These hydrogen-bond networks are a conserved feature of the crotonase oxyanion hole and their importance for catalysis is discussed.","PeriodicalId":6895,"journal":{"name":"Acta Crystallographica Section D: Biological Crystallography","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2015-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80741889","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 6

Selecting soluble/foldable protein domains through single-gene or genomic ORF filtering: structure of the head domain of Burkholderia pseudomallei antigen BPSL2063. 通过单基因或基因组ORF过滤选择可溶/可折叠蛋白结构域:伪伯克霍尔德菌抗原BPSL2063头部结构域的结构

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2015-11-01 DOI: 10.1107/S1399004715015680

L. Gourlay, C. Peano, C. Deantonio, L. Perletti, A. Pietrelli, R. Villa, Elena Matterazzo, P. Lassaux, C. Santoro, S. Puccio, D. Sblattero, M. Bolognesi

{"title":"Selecting soluble/foldable protein domains through single-gene or genomic ORF filtering: structure of the head domain of Burkholderia pseudomallei antigen BPSL2063.","authors":"L. Gourlay, C. Peano, C. Deantonio, L. Perletti, A. Pietrelli, R. Villa, Elena Matterazzo, P. Lassaux, C. Santoro, S. Puccio, D. Sblattero, M. Bolognesi","doi":"10.1107/S1399004715015680","DOIUrl":"https://doi.org/10.1107/S1399004715015680","url":null,"abstract":"The 1.8 Å resolution crystal structure of a conserved domain of the potential Burkholderia pseudomallei antigen and trimeric autotransporter BPSL2063 is presented as a structural vaccinology target for melioidosis vaccine development. Since BPSL2063 (1090 amino acids) hosts only one conserved domain, and the expression/purification of the full-length protein proved to be problematic, a domain-filtering library was generated using β-lactamase as a reporter gene to select further BPSL2063 domains. As a result, two domains (D1 and D2) were identified and produced in soluble form in Escherichia coli. Furthermore, as a general tool, a genomic open reading frame-filtering library from the B. pseudomallei genome was also constructed to facilitate the selection of domain boundaries from the entire ORFeome. Such an approach allowed the selection of three potential protein antigens that were also produced in soluble form. The results imply the further development of ORF-filtering methods as a tool in protein-based research to improve the selection and production of soluble proteins or domains for downstream applications such as X-ray crystallography.","PeriodicalId":6895,"journal":{"name":"Acta Crystallographica Section D: Biological Crystallography","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2015-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85765017","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 9

Structural basis for the slow photocycle and late proton release in Acetabularia rhodopsin I from the marine plant Acetabularia acetabulum. 海洋植物髋臼紫红质I光循环慢、质子释放晚的结构基础。

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2015-11-01 DOI: 10.1107/S1399004715015722

M. Furuse, Jun Tamogami, T. Hosaka, T. Kikukawa, N. Shinya, M. Hato, N. Ohsawa, S. Kim, K. Jung, M. Demura, S. Miyauchi, N. Kamo, K. Shimono, T. Kimura-Someya, S. Yokoyama, M. Shirouzu

{"title":"Structural basis for the slow photocycle and late proton release in Acetabularia rhodopsin I from the marine plant Acetabularia acetabulum.","authors":"M. Furuse, Jun Tamogami, T. Hosaka, T. Kikukawa, N. Shinya, M. Hato, N. Ohsawa, S. Kim, K. Jung, M. Demura, S. Miyauchi, N. Kamo, K. Shimono, T. Kimura-Someya, S. Yokoyama, M. Shirouzu","doi":"10.1107/S1399004715015722","DOIUrl":"https://doi.org/10.1107/S1399004715015722","url":null,"abstract":"Although many crystal structures of microbial rhodopsins have been solved, those with sufficient resolution to identify the functional water molecules are very limited. In this study, the Acetabularia rhodopsin I (ARI) protein derived from the marine alga A. acetabulum was synthesized on a large scale by the Escherichia coli cell-free membrane-protein production method, and crystal structures of ARI were determined at the second highest (1.52-1.80 Å) resolution for a microbial rhodopsin, following bacteriorhodopsin (BR). Examinations of the photochemical properties of ARI revealed that the photocycle of ARI is slower than that of BR and that its proton-transfer reactions are different from those of BR. In the present structures, a large cavity containing numerous water molecules exists on the extracellular side of ARI, explaining the relatively low pKa of Glu206(ARI), which cannot function as an initial proton-releasing residue at any pH. An interhelical hydrogen bond exists between Leu97(ARI) and Tyr221(ARI) on the cytoplasmic side, which facilitates the slow photocycle and regulates the pKa of Asp100(ARI), a potential proton donor to the Schiff base, in the dark state.","PeriodicalId":6895,"journal":{"name":"Acta Crystallographica Section D: Biological Crystallography","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2015-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85361849","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 19

Deformable complex network for refining low-resolution X-ray structures. 用于精炼低分辨率x射线结构的可变形复杂网络。

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2015-11-01 Epub Date: 2015-10-27 DOI: 10.1107/S139900471501528X

Chong Zhang, Qinghua Wang, Jianpeng Ma

引用次数: 1

Structural insight and flexible features of NS5 proteins from all four serotypes of Dengue virus in solution. 四种血清型登革热病毒 NS5 蛋白在溶液中的结构洞察力和柔性特征。

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2015-11-01 Epub Date: 2015-10-31 DOI: 10.1107/S1399004715017721

Wuan Geok Saw, Giancarlo Tria, Ardina Grüber, Malathy Sony Subramanian Manimekalai, Yongqian Zhao, Arun Chandramohan, Ganesh Srinivasan Anand, Tsutomu Matsui, Thomas M Weiss, Subhash G Vasudevan, Gerhard Grüber

{"title":"Structural insight and flexible features of NS5 proteins from all four serotypes of Dengue virus in solution.","authors":"Wuan Geok Saw, Giancarlo Tria, Ardina Grüber, Malathy Sony Subramanian Manimekalai, Yongqian Zhao, Arun Chandramohan, Ganesh Srinivasan Anand, Tsutomu Matsui, Thomas M Weiss, Subhash G Vasudevan, Gerhard Grüber","doi":"10.1107/S1399004715017721","DOIUrl":"10.1107/S1399004715017721","url":null,"abstract":"Infection by the four serotypes of Dengue virus (DENV-1 to DENV-4) causes an important arthropod-borne viral disease in humans. The multifunctional DENV nonstructural protein 5 (NS5) is essential for capping and replication of the viral RNA and harbours a methyltransferase (MTase) domain and an RNA-dependent RNA polymerase (RdRp) domain. In this study, insights into the overall structure and flexibility of the entire NS5 of all four Dengue virus serotypes in solution are presented for the first time. The solution models derived revealed an arrangement of the full-length NS5 (NS5FL) proteins with the MTase domain positioned at the top of the RdRP domain. The DENV-1 to DENV-4 NS5 forms are elongated and flexible in solution, with DENV-4 NS5 being more compact relative to NS5 from DENV-1, DENV-2 and DENV-3. Solution studies of the individual MTase and RdRp domains show the compactness of the RdRp domain as well as the contribution of the MTase domain and the ten-residue linker region to the flexibility of the entire NS5. Swapping the ten-residue linker between DENV-4 NS5FL and DENV-3 NS5FL demonstrated its importance in MTase-RdRp communication and in concerted interaction with viral and host proteins, as probed by amide hydrogen/deuterium mass spectrometry. Conformational alterations owing to RNA binding are presented. ","PeriodicalId":6895,"journal":{"name":"Acta Crystallographica Section D: Biological Crystallography","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2015-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4631481/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79085556","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex. 结核分枝杆菌邻氨基甲酸合酶复合体I亚基的结构、抑制及活性复合体的表达。

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2015-11-01 DOI: 10.1107/S1399004715017216

G. Bashiri, J. Johnston, G. Evans, E. M. Bulloch, David C. Goldstone, E.N.M. Jirgis, S. Kleinboelting, A. Castell, R. J. Ramsay, Alexandra Manos-Turvey, Richard J. Payne, J. Lott, Edward N. Baker

{"title":"Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex.","authors":"G. Bashiri, J. Johnston, G. Evans, E. M. Bulloch, David C. Goldstone, E.N.M. Jirgis, S. Kleinboelting, A. Castell, R. J. Ramsay, Alexandra Manos-Turvey, Richard J. Payne, J. Lott, Edward N. Baker","doi":"10.1107/S1399004715017216","DOIUrl":"https://doi.org/10.1107/S1399004715017216","url":null,"abstract":"The tryptophan-biosynthesis pathway is essential for Mycobacterium tuberculosis (Mtb) to cause disease, but not all of the enzymes that catalyse this pathway in this organism have been identified. The structure and function of the enzyme complex that catalyses the first committed step in the pathway, the anthranilate synthase (AS) complex, have been analysed. It is shown that the open reading frames Rv1609 (trpE) and Rv0013 (trpG) encode the chorismate-utilizing (AS-I) and glutamine amidotransferase (AS-II) subunits of the AS complex, respectively. Biochemical assays show that when these subunits are co-expressed a bifunctional AS complex is obtained. Crystallization trials on Mtb-AS unexpectedly gave crystals containing only AS-I, presumably owing to its selective crystallization from solutions containing a mixture of the AS complex and free AS-I. The three-dimensional structure reveals that Mtb-AS-I dimerizes via an interface that has not previously been seen in AS complexes. As is the case in other bacteria, it is demonstrated that Mtb-AS shows cooperative allosteric inhibition by tryptophan, which can be rationalized based on interactions at this interface. Comparative inhibition studies on Mtb-AS-I and related enzymes highlight the potential for single inhibitory compounds to target multiple chorismate-utilizing enzymes for TB drug discovery.","PeriodicalId":6895,"journal":{"name":"Acta Crystallographica Section D: Biological Crystallography","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2015-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87516121","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 17

Crystallographic study of a MATE transporter presents a difficult case in structure determination with low-resolution, anisotropic data and crystal twinning. 在低分辨率、各向异性数据和晶体孪晶的情况下，MATE转运体的晶体学研究在结构确定方面存在困难。

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2015-11-01 DOI: 10.1107/S1399004715016995

J. Symerský, Yi Guo, Jimin Wang, Min Lu

引用次数: 1

The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer-Villiger monooxygenase. 来自假单胞菌 CAM 质粒的 3,6-二酮樟脑单加氧酶的加氧成分：II 型 Baeyer-Villiger 单加氧酶的首个晶体结构。

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2015-11-01 Epub Date: 2015-10-31 DOI: 10.1107/S1399004715017939

Michail N Isupov, Ewald Schröder, Robert P Gibson, Jean Beecher, Giuliana Donadio, Vahid Saneei, Stephlina A Dcunha, Emma J McGhie, Christopher Sayer, Colin F Davenport, Peter C Lau, Yoshie Hasegawa, Hiroaki Iwaki, Maria Kadow, Kathleen Balke, Uwe T Bornscheuer, Gleb Bourenkov, Jennifer A Littlechild

{"title":"The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer-Villiger monooxygenase.","authors":"Michail N Isupov, Ewald Schröder, Robert P Gibson, Jean Beecher, Giuliana Donadio, Vahid Saneei, Stephlina A Dcunha, Emma J McGhie, Christopher Sayer, Colin F Davenport, Peter C Lau, Yoshie Hasegawa, Hiroaki Iwaki, Maria Kadow, Kathleen Balke, Uwe T Bornscheuer, Gleb Bourenkov, Jennifer A Littlechild","doi":"10.1107/S1399004715017939","DOIUrl":"10.1107/S1399004715017939","url":null,"abstract":"The three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer-Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 Å resolution. The structure of this dimeric FMN-dependent enzyme, which is encoded on the large CAM plasmid of Pseudomonas putida, has been solved by a combination of multiple anomalous dispersion from a bromine crystal soak and molecular replacement using a bacterial luciferase model. The orientation of the isoalloxazine ring of the FMN cofactor in the active site of this TIM-barrel fold enzyme differs significantly from that previously observed in enzymes of the bacterial luciferase-like superfamily. The Ala77 residue is in a cis conformation and forms a β-bulge at the C-terminus of β-strand 3, which is a feature observed in many proteins of this superfamily.","PeriodicalId":6895,"journal":{"name":"Acta Crystallographica Section D: Biological Crystallography","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2015-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4631483/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"61948478","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3'')(9) adenyltransferase. 肠道沙门氏菌AadA的结构:一个单体氨基糖苷(3”)(9)腺苷转移酶。

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2015-11-01 Epub Date: 2015-10-31 DOI: 10.1107/S1399004715016429

Yang Chen, Joakim Näsvall, Shiying Wu, Dan I Andersson, Maria Selmer

{"title":"Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3'')(9) adenyltransferase.","authors":"Yang Chen, Joakim Näsvall, Shiying Wu, Dan I Andersson, Maria Selmer","doi":"10.1107/S1399004715016429","DOIUrl":"10.1107/S1399004715016429","url":null,"abstract":"Aminoglycoside resistance is commonly conferred by enzymatic modification of drugs by aminoglycoside-modifying enzymes such as aminoglycoside nucleotidyltransferases (ANTs). Here, the first crystal structure of an ANT(3'')(9) adenyltransferase, AadA from Salmonella enterica, is presented. AadA catalyses the magnesium-dependent transfer of adenosine monophosphate from ATP to the two chemically dissimilar drugs streptomycin and spectinomycin. The structure was solved using selenium SAD phasing and refined to 2.5 Å resolution. AadA consists of a nucleotidyltransferase domain and an α-helical bundle domain. AadA crystallizes as a monomer and is a monomer in solution as confirmed by small-angle X-ray scattering, in contrast to structurally similar homodimeric adenylating enzymes such as kanamycin nucleotidyltransferase. Isothermal titration calorimetry experiments show that ATP binding has to occur before binding of the aminoglycoside substrate, and structure analysis suggests that ATP binding repositions the two domains for aminoglycoside binding in the interdomain cleft. Candidate residues for ligand binding and catalysis were subjected to site-directed mutagenesis. In vivo resistance and in vitro binding assays support the role of Glu87 as the catalytic base in adenylation, while Arg192 and Lys205 are shown to be critical for ATP binding.","PeriodicalId":6895,"journal":{"name":"Acta Crystallographica Section D: Biological Crystallography","volume":null,"pages":null},"PeriodicalIF":2.2,"publicationDate":"2015-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715016429","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"61948413","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 16