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":"327 1","pages":""},"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}
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":"55 1","pages":"65-71"},"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}
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":"22 1","pages":"14-22"},"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}
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":"39 1","pages":"1309-1317"},"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}
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":"28 1","pages":"512-519"},"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}
{"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":"69 Pt 12","pages":"1315"},"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}
{"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":"69 Pt 12","pages":"1411-4"},"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}
{"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":"69 Pt 12","pages":"1339-43"},"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}
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, Peng-Chao Guo, Jin-Di Ma, 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":"69 Pt 11","pages":"1190-5"},"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}
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":"69 Pt 11","pages":"1239-41"},"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}