Acta crystallographica. Section D, Biological crystallography最新文献_第8页

Structural and biochemical analyses of a Clostridium perfringens sortase D transpeptidase. 产气荚膜梭菌分选酶D转肽酶的结构和生化分析。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-07-01 Epub Date: 2015-06-30 DOI: 10.1107/S1399004715009219

Randy Suryadinata, Shane A Seabrook, Timothy E Adams, Stewart D Nuttall, Thomas S Peat

{"title":"Structural and biochemical analyses of a Clostridium perfringens sortase D transpeptidase.","authors":"Randy Suryadinata, Shane A Seabrook, Timothy E Adams, Stewart D Nuttall, Thomas S Peat","doi":"10.1107/S1399004715009219","DOIUrl":"10.1107/S1399004715009219","url":null,"abstract":"The assembly and anchorage of various pathogenic proteins on the surface of Gram-positive bacteria is mediated by the sortase family of enzymes. These cysteine transpeptidases catalyze a unique sorting signal motif located at the C-terminus of their target substrate and promote the covalent attachment of these proteins onto an amino nucleophile located on another protein or on the bacterial cell wall. Each of the six distinct classes of sortases displays a unique biological role, with sequential activation of multiple sortases often observed in many Gram-positive bacteria to decorate their peptidoglycans. Less is known about the members of the class D family of sortases (SrtD), but they have a suggested role in spore formation in an oxygen-limiting environment. Here, the crystal structure of the SrtD enzyme from Clostridium perfringens was determined at 1.99 Å resolution. Comparative analysis of the C. perfringens SrtD structure reveals the typical eight-stranded β-barrel fold observed in all other known sortases, along with the conserved catalytic triad consisting of cysteine, histidine and arginine residues. Biochemical approaches further reveal the specifics of the SrtD catalytic activity in vitro, with a significant preference for the LPQTGS sorting motif. Additionally, the catalytic activity of SrtD is most efficient at 316 K and can be further improved in the presence of magnesium cations. Since C. perfringens spores are heat-resistant and lead to foodborne illnesses, characterization of the spore-promoting sortase SrtD may lead to the development of new antimicrobial agents.","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":" ","pages":"1505-13"},"PeriodicalIF":0.0,"publicationDate":"2015-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715009219","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34262930","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: 14

Structural characterization of a novel subfamily of leucine-rich repeat proteins from the human pathogen Leptospira interrogans. 来自人类病原体钩端螺旋体的富含亮氨酸重复蛋白的新亚家族的结构特征。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-06-01 Epub Date: 2015-05-23 DOI: 10.1107/S139900471500704X

Isabelle Miras, Frederick Saul, Mireille Nowakowski, Patrick Weber, Ahmed Haouz, William Shepard, Mathieu Picardeau

{"title":"Structural characterization of a novel subfamily of leucine-rich repeat proteins from the human pathogen Leptospira interrogans.","authors":"Isabelle Miras, Frederick Saul, Mireille Nowakowski, Patrick Weber, Ahmed Haouz, William Shepard, Mathieu Picardeau","doi":"10.1107/S139900471500704X","DOIUrl":"https://doi.org/10.1107/S139900471500704X","url":null,"abstract":"Pathogenic Leptospira spp. are the agents of leptospirosis, an emerging zoonotic disease. Analyses of Leptospira genomes have shown that the pathogenic leptospires (but not the saprophytes) possess a large number of genes encoding proteins containing leucine-rich repeat (LRR) domains. In other pathogenic bacteria, proteins with LRR domains have been shown to be involved in mediating host-cell attachment and invasion, but their functions remain unknown in Leptospira. To gain insight into the potential function of leptospiral LRR proteins, the crystal structures of four LRR proteins that represent a novel subfamily with consecutive stretches of a 23-amino-acid LRR repeat motif have been solved. The four proteins analyzed adopt the characteristic α/β-solenoid horseshoe fold. The exposed residues of the inner concave surfaces of the solenoid, which constitute a putative functional binding site, are not conserved. The various leptospiral LRR proteins could therefore recognize distinct structural motifs of different host proteins and thus serve separate and complementary functions in the physiology of these bacteria. ","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 6","pages":"1351-9"},"PeriodicalIF":0.0,"publicationDate":"2015-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S139900471500704X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33253299","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: 20

Bond distances in polypeptide backbones depend on the local conformation. 多肽骨架的键距取决于局部构象。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-06-01 Epub Date: 2015-05-14 DOI: 10.1107/S1399004715005507

Roberto Improta, Luigi Vitagliano, Luciana Esposito

{"title":"Bond distances in polypeptide backbones depend on the local conformation.","authors":"Roberto Improta, Luigi Vitagliano, Luciana Esposito","doi":"10.1107/S1399004715005507","DOIUrl":"https://doi.org/10.1107/S1399004715005507","url":null,"abstract":"By combining quantum-mechanical analysis of small model peptides and statistical surveys of high-resolution protein structures, a systematic conformational dependence of bond lengths in polypeptide backbones has been unveiled which involves both the peptide bond (C-O and C-N) and those bonds centred on the C(α) atom. All of these bond lengths indeed display a systematic variability in the ψ angle according to both calculations and surveys of protein structures. The overall agreement between the computed and the statistical data suggests that these trends are essentially driven by local effects. The dependence of C(α) distances on ψ is governed by interactions between the σ system of the C(α) moiety and the C-O π system of the peptide bond. Maximum and minimum values for each bond distance are found for conformations with the specific bond perpendicular and parallel to the adjacent CONH peptide plane, respectively. On the other hand, the variability of the C-O and C-N distances is related to the strength of the interactions between the lone pair of the N atom and the C-O π* system, which is modulated by the ψ angle. The C-O and C-N distances are related but their trends are not strictly connected to peptide-bond planarity, although a correlation amongst all of these parameters is expected on the basis of the classical resonance model. ","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 6","pages":"1272-83"},"PeriodicalIF":0.0,"publicationDate":"2015-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715005507","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33248376","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: 11

Two crystal structures of the FK506-binding domain of Plasmodium falciparum FKBP35 in complex with rapamycin at high resolution. 恶性疟原虫FKBP35与雷帕霉素复合物中fk506结合域的两种高分辨率晶体结构

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-06-01 Epub Date: 2015-05-14 DOI: 10.1107/S1399004715006239

Alessandra Bianchin, Frederic Allemand, Angus Bell, Anthony J Chubb, Jean François Guichou

{"title":"Two crystal structures of the FK506-binding domain of Plasmodium falciparum FKBP35 in complex with rapamycin at high resolution.","authors":"Alessandra Bianchin, Frederic Allemand, Angus Bell, Anthony J Chubb, Jean François Guichou","doi":"10.1107/S1399004715006239","DOIUrl":"https://doi.org/10.1107/S1399004715006239","url":null,"abstract":"Antimalarial chemotherapy continues to be challenging in view of the emergence of drug resistance, especially artemisinin resistance in Southeast Asia. It is critical that novel antimalarial drugs are identified that inhibit new targets with unexplored mechanisms of action. It has been demonstrated that the immunosuppressive drug rapamycin, which is currently in clinical use to prevent organ-transplant rejection, has antimalarial effects. The Plasmodium falciparum target protein is PfFKBP35, a unique immunophilin FK506-binding protein (FKBP). This protein family binds rapamycin, FK506 and other immunosuppressive and non-immunosuppressive macrolactones. Here, two crystallographic structures of rapamycin in complex with the FK506-binding domain of PfFKBP35 at high resolution, in both its oxidized and reduced forms, are reported. In comparison with the human FKBP12-rapamycin complex reported previously, the structures reveal differences in the β4-β6 segment that lines the rapamycin binding site. Structural differences between the Plasmodium protein and human hFKBP12 include the replacement of Cys106 and Ser109 by His87 and Ile90, respectively. The proximity of Cys106 to the bound rapamycin molecule (4-5 Å) suggests possible routes for the rational design of analogues of rapamycin with specific antiparasitic activity. Comparison of the structures with the PfFKBD-FK506 complex shows that both drugs interact with the same binding-site residues. These two new structures highlight the structural differences and the specific interactions that must be kept in consideration for the rational design of rapamycin analogues with antimalarial activity that specifically bind to PfFKBP35 without immunosuppressive effects.","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 6","pages":"1319-27"},"PeriodicalIF":0.0,"publicationDate":"2015-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715006239","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33248380","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: 13

Structure determination of an integral membrane protein at room temperature from crystals in situ. 利用原位晶体确定整体膜蛋白在室温下的结构。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-06-01 Epub Date: 2015-05-14 DOI: 10.1107/S139900471500423X

Danny Axford, James Foadi, Nien Jen Hu, Hassanul Ghani Choudhury, So Iwata, Konstantinos Beis, Gwyndaf Evans, Yilmaz Alguel

{"title":"Structure determination of an integral membrane protein at room temperature from crystals in situ.","authors":"Danny Axford, James Foadi, Nien Jen Hu, Hassanul Ghani Choudhury, So Iwata, Konstantinos Beis, Gwyndaf Evans, Yilmaz Alguel","doi":"10.1107/S139900471500423X","DOIUrl":"10.1107/S139900471500423X","url":null,"abstract":"The structure determination of an integral membrane protein using synchrotron X-ray diffraction data collected at room temperature directly in vapour-diffusion crystallization plates (in situ) is demonstrated. Exposing the crystals in situ eliminates manual sample handling and, since it is performed at room temperature, removes the complication of cryoprotection and potential structural anomalies induced by sample cryocooling. Essential to the method is the ability to limit radiation damage by recording a small amount of data per sample from many samples and subsequently assembling the resulting data sets using specialized software. The validity of this procedure is established by the structure determination of Haemophilus influenza TehA at 2.3 Å resolution. The method presented offers an effective protocol for the fast and efficient determination of membrane-protein structures at room temperature using third-generation synchrotron beamlines. ","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 6","pages":"1228-37"},"PeriodicalIF":0.0,"publicationDate":"2015-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4461203/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33374783","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

Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution. 牛COPI δ亚基μ同源域在2.15 Å分辨率下的结构。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-06-01 Epub Date: 2015-05-14 DOI: 10.1107/S1399004715006203

Avital Lahav, Haim Rozenberg, Anna Parnis, Dan Cassel, Noam Adir

{"title":"Structure of the bovine COPI δ subunit μ homology domain at 2.15 Å resolution.","authors":"Avital Lahav, Haim Rozenberg, Anna Parnis, Dan Cassel, Noam Adir","doi":"10.1107/S1399004715006203","DOIUrl":"https://doi.org/10.1107/S1399004715006203","url":null,"abstract":"The heptameric COPI coat (coatomer) plays an essential role in vesicular transport in the early secretory system of eukaryotic cells. While the structures of some of the subunits have been determined, that of the δ-COP subunit has not been reported to date. The δ-COP subunit is part of a subcomplex with structural similarity to tetrameric clathrin adaptors (APs), where δ-COP is the structural homologue of the AP μ subunit. Here, the crystal structure of the μ homology domain (MHD) of δ-COP (δ-MHD) obtained by phasing using a combined SAD-MR method is presented at 2.15 Å resolution. The crystallographic asymmetric unit contains two monomers that exhibit short sections of disorder, which may allude to flexible regions of the protein. The δ-MHD is composed of two subdomains connected by unstructured linkers. Comparison between this structure and those of known MHD domains from the APs shows significant differences in the positions of specific loops and β-sheets, as well as a more general change in the relative positions of the protein subdomains. The identified difference may be the major source of cargo-binding specificity. Finally, the crystal structure is used to analyze the potential effect of the I422T mutation in δ-COP previously reported to cause a neurodegenerative phenotype in mice.","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 6","pages":"1328-34"},"PeriodicalIF":0.0,"publicationDate":"2015-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715006203","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33248381","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: 6

Structural bases for N-glycan processing by mannoside phosphorylase. 甘露糖苷磷酸化酶加工n -聚糖的结构碱基。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-06-01 Epub Date: 2015-05-14 DOI: 10.1107/S1399004715006604

Simon Ladevèze, Gianluca Cioci, Pierre Roblin, Lionel Mourey, Samuel Tranier, Gabrielle Potocki-Véronèse

{"title":"Structural bases for N-glycan processing by mannoside phosphorylase.","authors":"Simon Ladevèze, Gianluca Cioci, Pierre Roblin, Lionel Mourey, Samuel Tranier, Gabrielle Potocki-Véronèse","doi":"10.1107/S1399004715006604","DOIUrl":"https://doi.org/10.1107/S1399004715006604","url":null,"abstract":"The first crystal structure of Uhgb_MP, a β-1,4-mannopyranosyl-chitobiose phosphorylase belonging to the GH130 family which is involved in N-glycan degradation by human gut bacteria, was solved at 1.85 Å resolution in the apo form and in complex with mannose and N-acetylglucosamine. SAXS and crystal structure analysis revealed a hexameric structure, a specific feature of GH130 enzymes among other glycoside phosphorylases. Mapping of the -1 and +1 subsites in the presence of phosphate confirmed the conserved Asp104 as the general acid/base catalytic residue, which is in agreement with a single-step reaction mechanism involving Man O3 assistance for proton transfer. Analysis of this structure, the first to be solved for a member of the GH130_2 subfamily, revealed Met67, Phe203 and the Gly121-Pro125 loop as the main determinants of the specificity of Uhgb_MP and its homologues towards the N-glycan core oligosaccharides and mannan, and the molecular bases of the key role played by GH130 enzymes in the catabolism of dietary fibre and host glycans.","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 6","pages":"1335-46"},"PeriodicalIF":0.0,"publicationDate":"2015-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715006604","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33248382","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: 16

Advances in membrane protein crystallography: in situ and in meso data collection. 膜蛋白晶体学的进展:原位和介观数据收集。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-06-01 Epub Date: 2015-05-23 DOI: 10.1107/S1399004715008317

Simone Weyand, Christopher G Tate

引用次数: 0

3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis DPN7(T): crystal structure and function of a desulfinase with an acyl-CoA dehydrogenase fold. 来自 Advenella mimigardefordensis DPN7(T) 的 3-亚磺酰丙酰基辅酶 A（3SP-CoA）脱硫酶：具有酰基辅酶脱氢酶折叠的脱硫酶的晶体结构和功能。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-06-01 Epub Date: 2015-05-23 DOI: 10.1107/S1399004715006616

Marc Schürmann, Rob Meijers, Thomas R Schneider, Alexander Steinbüchel, Michele Cianci

{"title":"3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase from Advenella mimigardefordensis DPN7(T): crystal structure and function of a desulfinase with an acyl-CoA dehydrogenase fold.","authors":"Marc Schürmann, Rob Meijers, Thomas R Schneider, Alexander Steinbüchel, Michele Cianci","doi":"10.1107/S1399004715006616","DOIUrl":"10.1107/S1399004715006616","url":null,"abstract":"3-Sulfinopropionyl-coenzyme A (3SP-CoA) desulfinase (AcdDPN7; EC 3.13.1.4) was identified during investigation of the 3,3'-dithiodipropionic acid (DTDP) catabolic pathway in the betaproteobacterium Advenella mimigardefordensis strain DPN7(T). DTDP is an organic disulfide and a precursor for the synthesis of polythioesters (PTEs) in bacteria, and is of interest for biotechnological PTE production. AcdDPN7 catalyzes sulfur abstraction from 3SP-CoA, a key step during the catabolism of DTDP. Here, the crystal structures of apo AcdDPN7 at 1.89 Å resolution and of its complex with the CoA moiety from the substrate analogue succinyl-CoA at 2.30 Å resolution are presented. The apo structure shows that AcdDPN7 belongs to the acyl-CoA dehydrogenase superfamily fold and that it is a tetramer, with each subunit containing one flavin adenine dinucleotide (FAD) molecule. The enzyme does not show any dehydrogenase activity. Dehydrogenase activity would require a catalytic base (Glu or Asp residue) at either position 246 or position 366, where a glutamine and a glycine are instead found, respectively, in this desulfinase. The positioning of CoA in the crystal complex enabled the modelling of a substrate complex containing 3SP-CoA. This indicates that Arg84 is a key residue in the desulfination reaction. An Arg84Lys mutant showed a complete loss of enzymatic activity, suggesting that the guanidinium group of the arginine is essential for desulfination. AcdDPN7 is the first desulfinase with an acyl-CoA dehydrogenase fold to be reported, which underlines the versatility of this enzyme scaffold.","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 6","pages":"1360-72"},"PeriodicalIF":0.0,"publicationDate":"2015-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4461206/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33253300","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 analysis of Dis3l2, an exosome-independent exonuclease from Schizosaccharomyces pombe. 裂糖菌非外泌体外切酶Dis3l2的结构分析。

Acta crystallographica. Section D, Biological crystallography Pub Date : 2015-06-01 Epub Date: 2015-05-14 DOI: 10.1107/S1399004715005805

Hui Lv, Yuwei Zhu, Yu Qiu, Liwen Niu, Maikun Teng, Xu Li

{"title":"Structural analysis of Dis3l2, an exosome-independent exonuclease from Schizosaccharomyces pombe.","authors":"Hui Lv, Yuwei Zhu, Yu Qiu, Liwen Niu, Maikun Teng, Xu Li","doi":"10.1107/S1399004715005805","DOIUrl":"https://doi.org/10.1107/S1399004715005805","url":null,"abstract":"After deadenylation and decapping, cytoplasmic mRNA can be digested in two opposite directions: in the 5'-3' direction by Xrn1 or in the 3'-5' direction by the exosome complex. Recently, a novel 3'-5' RNA-decay pathway involving Dis3l2 has been described that differs from degradation by Xrn1 and the exosome. The product of the Schizosaccharomyces pombe gene SPAC2C4.07c was identified as a homologue of human Dis3l2. In this work, the 2.8 Å resolution X-ray crystal structure of S. pombe Dis3l2 (SpDis3l2) is reported, the conformation of which is obviously different from that in the homologous mouse Dis3l2-RNA complex. Fluorescence polarization assay experiments showed that RNB and S1 are the primary RNA-binding domains and that the CSDs (CSD1 and CSD2) play an indispensable role in the RNA-binding process of SpDis3l2. Taking the structure comparison and mutagenic experiments together, it can be inferred that the RNA-recognition pattern of SpDis3l2 resembles that of its mouse homologue rather than that of the Escherichia coli RNase II-RNA complex. Furthermore, a drastic conformation change could occur following the binding of the RNA substrate to SpDis3l2.","PeriodicalId":7047,"journal":{"name":"Acta crystallographica. Section D, Biological crystallography","volume":"71 Pt 6","pages":"1284-94"},"PeriodicalIF":0.0,"publicationDate":"2015-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1399004715005805","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33248377","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: 11