1p5u
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1p5u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p5u, resolution 1.99Å" /> '''X-ray structure of t...) |
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| - | [[Image:1p5u.jpg|left|200px]]<br /><applet load="1p5u" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1p5u, resolution 1.99Å" /> | ||
| - | '''X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex'''<br /> | ||
| - | == | + | ==X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex== |
| - | Most gram-negative pathogens express fibrous adhesive virulence organelles | + | <StructureSection load='1p5u' size='340' side='right'caption='[[1p5u]], [[Resolution|resolution]] 1.99Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1p5u]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P5U FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.99Å</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=1p5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5u OCA], [https://pdbe.org/1p5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p5u RCSB], [https://www.ebi.ac.uk/pdbsum/1p5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p5u ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CAF1M_YERPE CAF1M_YERPE] Has a stimulatory role for the envelope antigen F1 secretion. It seems to interact with the subunit polypeptide and to prevent it from digestion by a protease. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p5/1p5u_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1p5u ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection. The F1 capsular antigen from the plague pathogen Yersinia pestis consists of linear fibers of a single subunit (Caf1) and serves as a prototype for nonpilus organelles assembled via the chaperone/usher pathway. Genetic data together with high-resolution X-ray structures corresponding to snapshots of the assembly process reveal the structural basis of fiber formation. Comparison of chaperone bound Caf1 subunit with the subunit in the fiber reveals a novel type of conformational change involving the entire hydrophobic core of the protein. The observed conformational change suggests that the chaperone traps a high-energy folding intermediate of Caf1. A model is proposed in which release of the subunit allows folding to be completed, driving fiber formation. | ||
| - | + | Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation.,Zavialov AV, Berglund J, Pudney AF, Fooks LJ, Ibrahim TM, MacIntyre S, Knight SD Cell. 2003 May 30;113(5):587-96. PMID:12787500<ref>PMID:12787500</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1p5u" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Yersinia pestis]] | [[Category: Yersinia pestis]] | ||
| - | [[Category: Berglund | + | [[Category: Berglund J]] |
| - | [[Category: Fooks | + | [[Category: Fooks LJ]] |
| - | [[Category: Ibrahim | + | [[Category: Ibrahim TM]] |
| - | [[Category: Knight | + | [[Category: Knight SD]] |
| - | [[Category: MacIntyre | + | [[Category: MacIntyre S]] |
| - | [[Category: Pudney | + | [[Category: Pudney AF]] |
| - | [[Category: Zavialov | + | [[Category: Zavialov AV]] |
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Current revision
X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex
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