4XVW

Crystal structure of Proteus mirabilis ScsC in a compact conformation

Summary for 4XVW

• Entry DOI: 10.2210/pdb4xvw/pdb
• Descriptor: DsbA-like protein (2 entities in total)
• Functional Keywords: thioredoxin fold, disulfide isomerase, trimeric, antimicrobial resistance, swarming motility, isomerase
• Biological source: Proteus mirabilis ATCC 29906
• Total number of polymer chains: 24
• Total formula weight: 599712.50

Authors

Kurth, F.,Furlong, E.J.,Premkumar, L.,Martin, J.L. (deposition date: 2015-01-27, release date: 2016-06-08, Last modification date: 2024-10-09)

Primary citation

Furlong, E.J.,Lo, A.W.,Kurth, F.,Premkumar, L.,Totsika, M.,Achard, M.E.S.,Halili, M.A.,Heras, B.,Whitten, A.E.,Choudhury, H.G.,Schembri, M.A.,Martin, J.L.
A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance.
Nat Commun, 8:16065-16065, 2017

PubMed Abstract: 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.

PubMed: 28722010
DOI: 10.1038/ncomms16065

Experimental method

X-RAY DIFFRACTION (2.6 Å)