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EPSP synthase from Acinetobacter baumannii 鲍曼不动杆菌EPSP合成酶
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2016-02-24 DOI: 10.2210/PDB5BS5/PDB
K. Sutton, L. Schultz, T. Russo, J. Breen, T. Umland
{"title":"EPSP synthase from Acinetobacter baumannii","authors":"K. Sutton, L. Schultz, T. Russo, J. Breen, T. Umland","doi":"10.2210/PDB5BS5/PDB","DOIUrl":"https://doi.org/10.2210/PDB5BS5/PDB","url":null,"abstract":"","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2016-02-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80399924","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: 0
Structure of methionine gamma-lyase from Clostridium sporogenes. 产孢梭菌蛋氨酸裂解酶的结构。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2016-01-13 DOI: 10.2210/PDB5DX5/PDB
S. Revtovich, N. Anufrieva, E. Morozova, Kulikova, A. Nikulin, T. Demidkina
{"title":"Structure of methionine gamma-lyase from Clostridium sporogenes.","authors":"S. Revtovich, N. Anufrieva, E. Morozova, Kulikova, A. Nikulin, T. Demidkina","doi":"10.2210/PDB5DX5/PDB","DOIUrl":"https://doi.org/10.2210/PDB5DX5/PDB","url":null,"abstract":"","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2016-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74954640","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: 0
Structure of aspartate b-semialdehyde dehydrogenase from Francisella tularensis 土拉弗朗西斯菌天冬氨酸b-半醛脱氢酶的结构
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2015-10-21 DOI: 10.2210/pdb4woj/pdb
N. Mank, S. Pote, K. Majorek, A. Arnette, V. Klapper, B. Hurlburt, M. Chruszcz
{"title":"Structure of aspartate b-semialdehyde dehydrogenase from Francisella tularensis","authors":"N. Mank, S. Pote, K. Majorek, A. Arnette, V. Klapper, B. Hurlburt, M. Chruszcz","doi":"10.2210/pdb4woj/pdb","DOIUrl":"https://doi.org/10.2210/pdb4woj/pdb","url":null,"abstract":"","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2015-10-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91121734","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: 1
Structure of a catalytic dimer of the alpha- and beta-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 angstrom resolution. 反硝化副球菌f - atp酶α亚基和β亚基催化二聚体在2.3埃分辨率下的结构。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2015-10-07 DOI: 10.2210/PDB5CDF/PDB
E. Morales-Ríos, M. G. Montgomery, A. Leslie, José J García-Trejo, J. Walker
{"title":"Structure of a catalytic dimer of the alpha- and beta-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 angstrom resolution.","authors":"E. Morales-Ríos, M. G. Montgomery, A. Leslie, José J García-Trejo, J. Walker","doi":"10.2210/PDB5CDF/PDB","DOIUrl":"https://doi.org/10.2210/PDB5CDF/PDB","url":null,"abstract":"","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2015-10-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84552966","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: 1
Grappling with anisotropic data, pseudo-merohedral twinning and pseudo-translational noncrystallographic symmetry: a case study involving pyruvate kinase 处理各向异性数据，伪面体孪生和伪平移非晶体对称:一个涉及丙酮酸激酶的案例研究
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2015-03-25 DOI: 10.2210/PDB4YNG/PDB
K. Donovan, Sarah C Atkinson, S. Kessans, Fen Peng, T. Cooper, M. Griffin, G. Jameson, R. Dobson
{"title":"Grappling with anisotropic data, pseudo-merohedral twinning and pseudo-translational noncrystallographic symmetry: a case study involving pyruvate kinase","authors":"K. Donovan, Sarah C Atkinson, S. Kessans, Fen Peng, T. Cooper, M. Griffin, G. Jameson, R. Dobson","doi":"10.2210/PDB4YNG/PDB","DOIUrl":"https://doi.org/10.2210/PDB4YNG/PDB","url":null,"abstract":"Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Private Bag 4800, Christchurch 8041, New Zealand, Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Melbourne, Victoria, Australia, Department of Biology and Biochemistry, University of Houston, Houston, TX 77204, USA, Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, 30 Flemington Road, Parkville, Victoria 3010, Australia, and Institute of Fundamental Sciences, Massey University, PO Box 11-222, Palmerston North 4442, New Zealand. *Correspondence e-mail: renwick.dobson@canterbury.ac.nz","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2015-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83303370","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: 7
Big changes are ahead--a new format for crystallization communications in Acta Cryst. F. 大的变化就在前面——《晶体学报》中出现了结晶通信的新格式。F。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-12-01 Epub Date: 2013-11-30 DOI: 10.1107/S1744309113031990
Manfred S Weiss, Howard Einspahr
{"title":"Big changes are ahead--a new format for crystallization communications in Acta Cryst. F.","authors":"Manfred S Weiss, Howard Einspahr","doi":"10.1107/S1744309113031990","DOIUrl":"https://doi.org/10.1107/S1744309113031990","url":null,"abstract":"The Editors of Acta F look forward to 2014.","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2013-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1744309113031990","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31937694","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: 1
Crystallization and preliminary X-ray crystallographic analysis of the inhibitory domain of the tomato mosaic virus resistance protein Tm-1. 番茄花叶病毒抗性蛋白 Tm-1 的抑制结构域的结晶和初步 X 射线晶体学分析。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-12-01 Epub Date: 2013-11-29 DOI: 10.1107/S1744309113030819
Masahiko Kato, Yuichiro Kezuka, Chihoko Kobayashi, Kazuhiro Ishibashi, Takamasa Nonaka, Masayuki Ishikawa, Estuko Katoh
{"title":"Crystallization and preliminary X-ray crystallographic analysis of the inhibitory domain of the tomato mosaic virus resistance protein Tm-1.","authors":"Masahiko Kato, Yuichiro Kezuka, Chihoko Kobayashi, Kazuhiro Ishibashi, Takamasa Nonaka, Masayuki Ishikawa, Estuko Katoh","doi":"10.1107/S1744309113030819","DOIUrl":"10.1107/S1744309113030819","url":null,"abstract":"<p><p>Tm-1, an inhibitor protein of Tomato mosaic virus RNA replication, contains two conserved domains: an uncharacterized domain at its N-terminus and a TIM-barrel-like domain at its C-terminus. The N-terminal domain of Tm-1 has an inhibitory activity and its three-dimensional structure has not been determined. Here, the crystallization and preliminary X-ray diffraction of the N-terminal domain of Tm-1 are reported. A three-wavelength MAD data set was collected from a selenomethionine-labelled crystal and processed to 2.7 Å resolution. The crystal belonged to the triclinic space group P1, with unit-cell parameters a = 77.97, b = 105.28, c = 110.62 Å, α = 94.6, β = 109.3, γ = 108.0°.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2013-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3855732/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31936950","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
Two high-resolution structures of the human E3 ubiquitin ligase Siah1. 人E3泛素连接酶Siah1的两个高分辨率结构。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-12-01 Epub Date: 2013-11-28 DOI: 10.1107/S1744309113031448
Vadim Rimsa, Thomas C Eadsforth, William N Hunter
{"title":"Two high-resolution structures of the human E3 ubiquitin ligase Siah1.","authors":"Vadim Rimsa, Thomas C Eadsforth, William N Hunter","doi":"10.1107/S1744309113031448","DOIUrl":"10.1107/S1744309113031448","url":null,"abstract":"<p><p>Siah1 is an E3 ubiquitin ligase that contributes to proteasome-mediated degradation of multiple targets in key cellular processes and which shows promise as a therapeutic target in oncology. Structures of a truncated Siah1 bound to peptide-based inhibitors have been reported. Here, new crystallization conditions have allowed the determination of a construct encompassing dual zinc-finger subdomains and substrate-binding domains at significantly higher resolution. Although the crystals appear isomorphous, two structures present distinct states in which the spatial orientation of one zinc-finger subdomain differs with respect to the rest of the dimeric protein. Such a difference, which is indicative of conformational freedom, infers potential biological relevance related to recognition of binding partners. The crystallization conditions and improved models of Siah1 may aid future studies investigating Siah1-ligand complexes. </p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2013-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1744309113031448","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31936039","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: 10
Structures of Saccharomyces cerevisiae D-arabinose dehydrogenase Ara1 and its complex with NADPH: implications for cofactor-assisted substrate recognition. 酿酒酵母d -阿拉伯糖脱氢酶Ara1的结构及其与NADPH的复合物:对辅因子辅助底物识别的意义。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-11-01 Epub Date: 2013-10-26 DOI: 10.1107/S1744309113026857
Xiao-Qian Hu, Peng-Chao Guo, Jin-Di Ma, Wei-Fang Li
{"title":"Structures of Saccharomyces cerevisiae D-arabinose dehydrogenase Ara1 and its complex with NADPH: implications for cofactor-assisted substrate recognition.","authors":"Xiao-Qian Hu,&nbsp;Peng-Chao Guo,&nbsp;Jin-Di Ma,&nbsp;Wei-Fang Li","doi":"10.1107/S1744309113026857","DOIUrl":"https://doi.org/10.1107/S1744309113026857","url":null,"abstract":"<p><p>The primary role of yeast Ara1, previously mis-annotated as a D-arabinose dehydrogenase, is to catalyze the reduction of a variety of toxic α,β-dicarbonyl compounds using NADPH as a cofactor at physiological pH levels. Here, crystal structures of Ara1 in apo and NADPH-complexed forms are presented at 2.10 and 2.00 Å resolution, respectively. Ara1 exists as a homodimer, each subunit of which adopts an (α/β)8-barrel structure and has a highly conserved cofactor-binding pocket. Structural comparison revealed that induced fit upon NADPH binding yielded an intact active-site pocket that recognizes the substrate. Moreover, the crystal structures combined with computational simulation defined an open substrate-binding site to accommodate various substrates that possess a dicarbonyl group. </p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2013-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1107/S1744309113026857","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31832720","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: 4
12-Fold symmetry of the putative portal protein from the Thermus thermophilus bacteriophage G20C determined by X-ray analysis. 通过 X 射线分析确定的嗜热菌噬菌体 G20C 假定门户蛋白的 12 倍对称性。
IF 0.9 4区 生物学
Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2013-11-01 Epub Date: 2013-10-17 DOI: 10.1107/S174430911302486X
Lowri S Williams, Vladimir M Levdikov, Leonid Minakhin, Konstantin Severinov, Alfred A Antson
{"title":"12-Fold symmetry of the putative portal protein from the Thermus thermophilus bacteriophage G20C determined by X-ray analysis.","authors":"Lowri S Williams, Vladimir M Levdikov, Leonid Minakhin, Konstantin Severinov, Alfred A Antson","doi":"10.1107/S174430911302486X","DOIUrl":"10.1107/S174430911302486X","url":null,"abstract":"<p><p>In tailed bacteriophages and several animal viruses, the portal protein forms the gateway through which viral DNA is translocated into the head structure during viral particle assembly. In the mature virion the portal protein exists as a dodecamer, while recombinant portal proteins from several phages, including SPP1 and CNPH82, have been shown to form 13-subunit assemblies. A putative portal protein from the thermostable bacteriophage G20C has been cloned, overexpressed and purified. Crystals of the protein diffracted to 2.1 Å resolution and belonged to space group P42(1)2, with unit-cell parameters a = b = 155.3, c = 115.4 Å. The unit-cell content and self-rotation function calculations indicate that the protein forms a circular 12-subunit assembly.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9,"publicationDate":"2013-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3818042/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31834275","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
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