3vor: Difference between revisions
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<StructureSection load='3vor' size='340' side='right'caption='[[3vor]], [[Resolution|resolution]] 0.90Å' scene=''> | <StructureSection load='3vor' size='340' side='right'caption='[[3vor]], [[Resolution|resolution]] 0.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3vor]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3vor]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VOR FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.9Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vor OCA], [https://pdbe.org/3vor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vor RCSB], [https://www.ebi.ac.uk/pdbsum/3vor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vor ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vor OCA], [https://pdbe.org/3vor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vor RCSB], [https://www.ebi.ac.uk/pdbsum/3vor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vor ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q59393_ECOLX Q59393_ECOLX] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Baba | [[Category: Baba S]] | ||
[[Category: Fukakusa | [[Category: Fukakusa S]] | ||
[[Category: Honda | [[Category: Honda T]] | ||
[[Category: Iida | [[Category: Iida T]] | ||
[[Category: Iwasita | [[Category: Iwasita T]] | ||
[[Category: Kawahara | [[Category: Kawahara K]] | ||
[[Category: Kobayashi | [[Category: Kobayashi Y]] | ||
[[Category: Nakamura | [[Category: Nakamura S]] | ||
[[Category: Nishimura | [[Category: Nishimura M]] | ||
[[Category: Ohkubo | [[Category: Ohkubo T]] | ||
[[Category: Taniguchi | [[Category: Taniguchi T]] | ||
Latest revision as of 12:48, 30 October 2024
Crystal Structure Analysis of the CofACrystal Structure Analysis of the CofA
Structural highlights
FunctionPublication Abstract from PubMedCofA, a major pilin subunit of colonization factor antigen III (CFA/III), forms pili that mediate small-intestinal colonization by enterotoxigenic Escherichia coli (ETEC). In this study, the crystal structure of an N-terminally truncated version of CofA was determined by single-wavelength anomalous diffraction (SAD) phasing using five sulfurs in the protein. Given the counterbalance between anomalous signal strength and the undesired X-ray absorption of the solvent, diffraction data were collected at 1.5 A resolution using synchrotron radiation. These data were sufficient to elucidate the sulfur substructure at 1.38 A resolution. The low solvent content (29%) of the crystal necessitated that density modification be performed with an additional 0.9 A resolution data set to reduce the phase error caused by the small sulfur anomalous signal. The CofA structure showed the alphabeta-fold typical of type IVb pilins and showed high structural homology to that of TcpA for toxin-coregulated pili of Vibrio cholerae, including spatial distribution of key residues critical for pilin self-assembly. A pilus-filament model of CofA was built by computational docking and molecular-dynamics simulation using the previously reported filament model of TcpA as a structural template. This model revealed that the CofA filament surface was highly negatively charged and that a 23-residue-long loop between the alpha1 and alpha2 helices filled the gap between the pilin subunits. These characteristics could provide a unique binding epitope for the CFA/III pili of ETEC compared with other type IVb pili. Structure of the CFA/III major pilin subunit CofA from human enterotoxigenic Escherichia coli determined at 0.90 A resolution by sulfur-SAD phasing.,Fukakusa S, Kawahara K, Nakamura S, Iwashita T, Baba S, Nishimura M, Kobayashi Y, Honda T, Iida T, Taniguchi T, Ohkubo T Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1418-29. Epub 2012 Sep, 13. PMID:22993096[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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