2m1n: Difference between revisions
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==Solution structure of a chaperone in type III secretion system== | ==Solution structure of a chaperone in type III secretion system== | ||
<StructureSection load='2m1n' size='340' side='right' caption='[[2m1n | <StructureSection load='2m1n' size='340' side='right'caption='[[2m1n]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2m1n]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2m1n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_3003 Escherichia coli 3003]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M1N 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">Solution NMR</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=2m1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m1n OCA], [https://pdbe.org/2m1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m1n RCSB], [https://www.ebi.ac.uk/pdbsum/2m1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m1n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli 3003]] | [[Category: Escherichia coli 3003]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Chen L]] | ||
[[Category: | [[Category: Economou A]] | ||
[[Category: | [[Category: Kalodimos C]] | ||
Latest revision as of 08:57, 15 May 2024
Solution structure of a chaperone in type III secretion systemSolution structure of a chaperone in type III secretion system
Structural highlights
Publication Abstract from PubMedThe targeting of type III secretion (TTS) proteins at the injectisome is an important process in bacterial virulence. Nevertheless, how the injectisome specifically recognizes TTS substrates among all bacterial proteins is unknown. A TTS peripheral membrane ATPase protein located at the base of the injectisome has been implicated in the targeting process. We have investigated the targeting of the EspA filament protein and its cognate chaperone, CesAB, to the EscN ATPase of the enteropathogenic E. coli (EPEC). We show that EscN selectively engages the EspA-loaded CesAB but not the unliganded CesAB. Structure analysis revealed that the targeting signal is encoded in a disorder-order structural transition in CesAB that is elicited only upon the binding of its physiological substrate, EspA. Abrogation of the interaction between the CesAB-EspA complex and EscN resulted in severe secretion and infection defects. Additionally, we show that the targeting and secretion signals are distinct and that the two processes are likely regulated by different mechanisms. Substrate-Activated Conformational Switch on Chaperones Encodes a Targeting Signal in Type III Secretion.,Chen L, Ai X, Portaliou AG, Minetti CA, Remeta DP, Economou A, Kalodimos CG Cell Rep. 2013 Mar 28;3(3):709-15. doi: 10.1016/j.celrep.2013.02.025. Epub 2013, Mar 21. PMID:23523349[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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