View source for 5idr


==Crystal structure of Proteus Mirabilis ScsC in a transitional conformation==
<StructureSection load='5idr' size='340' side='right'caption='[[5idr]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5idr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_mirabilis_ATCC_29906 Proteus mirabilis ATCC 29906]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IDR 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]] 2.562&#8491;</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=5idr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5idr OCA], [https://pdbe.org/5idr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5idr RCSB], [https://www.ebi.ac.uk/pdbsum/5idr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5idr ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Copper resistance is a key virulence trait of the uropathogen Proteus mirabilis. Here we show that P. mirabilis ScsC (PmScsC) contributes to this defence mechanism by enabling swarming in the presence of copper. We also demonstrate that PmScsC is a thioredoxin-like disulfide isomerase but, unlike other characterized proteins in this family, it is trimeric. PmScsC trimerization and its active site cysteine are required for wild-type swarming activity in the presence of copper. Moreover, PmScsC exhibits unprecedented motion as a consequence of a shape-shifting motif linking the catalytic and trimerization domains. The linker accesses strand, loop and helical conformations enabling the sampling of an enormous folding landscape by the catalytic domains. Mutation of the shape-shifting motif abolishes disulfide isomerase activity, as does removal of the trimerization domain, showing that both features are essential to foldase function. More broadly, the shape-shifter peptide has the potential for 'plug and play' application in protein engineering.

A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance.,Furlong EJ, Lo AW, Kurth F, Premkumar L, Totsika M, Achard MES, Halili MA, Heras B, Whitten AE, Choudhury HG, Schembri MA, Martin JL Nat Commun. 2017 Jul 19;8:16065. doi: 10.1038/ncomms16065. PMID:28722010<ref>PMID:28722010</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5idr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Proteus mirabilis ATCC 29906]]
[[Category: Choudhury HG]]
[[Category: Furlong EJ]]
[[Category: Kurth F]]
[[Category: Martin JL]]