A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance

Furlong, Emily J., Lo, Alvin W., Kurth, Fabian, Premkumar, Lakshmanane, Totsika, Makrina, Achard, Maud E. S., Halili, Maria A., Heras, Begona, Whitten, Andrew E., Choudhury, Hassanul G., Schembri, Mark A. and Martin, Jennifer L. (2017) A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance. Nature Communications, 8 . doi:10.1038/ncomms16065


Author Furlong, Emily J.
Lo, Alvin W.
Kurth, Fabian
Premkumar, Lakshmanane
Totsika, Makrina
Achard, Maud E. S.
Halili, Maria A.
Heras, Begona
Whitten, Andrew E.
Choudhury, Hassanul G.
Schembri, Mark A.
Martin, Jennifer L.
Title A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance
Formatted title
A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance
Journal name Nature Communications   Check publisher's open access policy
ISSN 2041-1723
Publication date 2017-07-19
Sub-type Article (original research)
DOI 10.1038/ncomms16065
Open Access Status DOI
Volume 8
Total pages 10
Place of publication London, United Kingdom
Publisher Nature Publishing Group
Language eng
Formatted 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.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ
Additional Notes Article number 16065

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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