4ayf: Difference between revisions
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==Crystal structure of the complex of the Caf1M:Caf1 chaperone:subunit preassembly complex carrying the Tyr40Ala mutation in the Caf1M chaperone== | ==Crystal structure of the complex of the Caf1M:Caf1 chaperone:subunit preassembly complex carrying the Tyr40Ala mutation in the Caf1M chaperone== | ||
<StructureSection load='4ayf' size='340' side='right' caption='[[4ayf]], [[Resolution|resolution]] 2.07Å' scene=''> | <StructureSection load='4ayf' size='340' side='right'caption='[[4ayf]], [[Resolution|resolution]] 2.07Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ayf]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ayf]] is a 2 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=4AYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AYF 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]] 2.07Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ayf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ayf OCA], [https://pdbe.org/4ayf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ayf RCSB], [https://www.ebi.ac.uk/pdbsum/4ayf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ayf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Yersinia pestis]] | ||
[[Category: | [[Category: Dubnovitsky A]] | ||
[[Category: Knight SD]] | |||
[[Category: | [[Category: MacIntyre S]] | ||
[[Category: | [[Category: Pudney AF]] | ||
[[Category: | [[Category: Yu XD]] | ||
[[Category: | [[Category: Zavialov AV]] | ||
[[Category: | |||
Latest revision as of 14:38, 20 December 2023
Crystal structure of the complex of the Caf1M:Caf1 chaperone:subunit preassembly complex carrying the Tyr40Ala mutation in the Caf1M chaperoneCrystal structure of the complex of the Caf1M:Caf1 chaperone:subunit preassembly complex carrying the Tyr40Ala mutation in the Caf1M chaperone
Structural highlights
FunctionCAF1M_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. Publication Abstract from PubMedMany virulence organelles of Gram-negative bacterial pathogens are assembled via the chaperone/usher pathway. The chaperone transports organelle subunits across the periplasm to the outer membrane usher, where they are released and incorporated into growing fibers. Here, we elucidate the mechanism of the usher-targeting step in assembly of the Yersinia pestis F1 capsule at the atomic level. The usher interacts almost exclusively with the chaperone in the chaperone:subunit complex. In free chaperone, a pair of conserved proline residues at the beginning of the subunit-binding loop form a "proline lock" that occludes the usher-binding surface and blocks usher binding. Binding of the subunit to the chaperone rotates the proline lock away from the usher-binding surface, allowing the chaperone-subunit complex to bind to the usher. We show that the proline lock exists in other chaperone/usher systems and represents a general allosteric mechanism for selective targeting of chaperone:subunit complexes to the usher and for release and recycling of the free chaperone. Allosteric Mechanism Controls Traffic in the Chaperone/Usher Pathway.,Di Yu X, Dubnovitsky A, Pudney AF, Macintyre S, Knight SD, Zavialov AV Structure. 2012 Sep 11. pii: S0969-2126(12)00298-5. doi:, 10.1016/j.str.2012.08.016. PMID:22981947[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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