4XVW

Crystal structure of Proteus mirabilis ScsC in a compact conformation

4XVW の概要

• エントリーDOI: 10.2210/pdb4xvw/pdb
• 分子名称: DsbA-like protein (2 entities in total)
• 機能のキーワード: thioredoxin fold, disulfide isomerase, trimeric, antimicrobial resistance, swarming motility, isomerase
• 由来する生物種: Proteus mirabilis ATCC 29906
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 599712.50

構造登録者

Kurth, F.,Furlong, E.J.,Premkumar, L.,Martin, J.L. (登録日: 2015-01-27, 公開日: 2016-06-08, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.6 Å)