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| | <StructureSection load='1z9s' size='340' side='right'caption='[[1z9s]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1z9s' size='340' side='right'caption='[[1z9s]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1z9s]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z9S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z9S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1z9s]] 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=1Z9S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z9S FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1p5u|1p5u]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">caf1M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900]), caf1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900])</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=1z9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z9s OCA], [https://pdbe.org/1z9s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z9s RCSB], [https://www.ebi.ac.uk/pdbsum/1z9s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z9s ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1z9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z9s OCA], [http://pdbe.org/1z9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z9s RCSB], [http://www.ebi.ac.uk/pdbsum/1z9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z9s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z9/1z9s_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z9/1z9s_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aqvist, J]] | + | [[Category: Yersinia pestis]] |
| - | [[Category: Brandsdal, B O]] | + | [[Category: Aqvist J]] |
| - | [[Category: Fooks, L J]] | + | [[Category: Brandsdal BO]] |
| - | [[Category: Knight, S D]] | + | [[Category: Fooks LJ]] |
| - | [[Category: Macintyre, S]] | + | [[Category: Knight SD]] |
| - | [[Category: Tischenko, V M]] | + | [[Category: Macintyre S]] |
| - | [[Category: Zavialov, A V]] | + | [[Category: Tischenko VM]] |
| - | [[Category: Yalov, V P.Zav]]
| + | [[Category: Zav'yalov VP]] |
| - | [[Category: Chaperone-immune system complex]] | + | [[Category: Zavialov AV]] |
| - | [[Category: Chaperone-usher pathway]]
| + | |
| - | [[Category: Donor strand complementation]]
| + | |
| - | [[Category: Native minimal fiber]]
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| Structural highlights
Function
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
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Periplasmic chaperone/usher machineries are used for assembly of filamentous adhesion organelles of Gram-negative pathogens in a process that has been suggested to be driven by folding energy. Structures of mutant chaperone-subunit complexes revealed a final folding transition (condensation of the subunit hydrophobic core) on the release of organelle subunit from the chaperone-subunit pre-assembly complex and incorporation into the final fibre structure. However, in view of the large interface between chaperone and subunit in the pre-assembly complex and the reported stability of this complex, it is difficult to understand how final folding could release sufficient energy to drive assembly. In the present paper, we show the X-ray structure for a native chaperone-fibre complex that, together with thermodynamic data, shows that the final folding step is indeed an essential component of the assembly process. We show that completion of the hydrophobic core and incorporation into the fibre results in an exceptionally stable module, whereas the chaperone-subunit pre-assembly complex is greatly destabilized by the high-energy conformation of the bound subunit. This difference in stabilities creates a free energy potential that drives fibre formation.
Resolving the energy paradox of chaperone/usher-mediated fibre assembly.,Zavialov AV, Tischenko VM, Fooks LJ, Brandsdal BO, Aqvist J, Zav'yalov VP, Macintyre S, Knight SD Biochem J. 2005 Aug 1;389(Pt 3):685-94. PMID:15799718[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zavialov AV, Tischenko VM, Fooks LJ, Brandsdal BO, Aqvist J, Zav'yalov VP, Macintyre S, Knight SD. Resolving the energy paradox of chaperone/usher-mediated fibre assembly. Biochem J. 2005 Aug 1;389(Pt 3):685-94. PMID:15799718 doi:10.1042/BJ20050426
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