Disulfide isomerase activity of the dynamic, trimeric Proteus mirabilis ScsC protein is primed by the tandem immunoglobulin-fold domain of ScsB

The Journal of Biological Chemistry
Emily J FurlongJennifer L Martin

Abstract

Correct disulfide bond formation is essential for proper folding of many proteins, including bacterial virulence factors. The suppressor of copper sensitivity (Scs) proteins have roles in dithiol/disulfide interchange and the bacterial response to copper stress. Encoded in a four-gene cassette (ScsABCD) present in many Gram-negative bacteria, the Scs proteins are enigmatic and poorly characterized. Here, we show that the periplasmic α-domain of the membrane protein ScsB in the Gram-negative bacterium Proteus mirabilis forms a redox relay with the soluble periplasmic protein PmScsC. We also found that the periplasmic α-domain is sufficient to activate the disulfide isomerase activity of PmScsC. The crystal structure of PmScsBα at a resolution of 1.54 Å revealed that it comprises two structurally similar immunoglobulin-like folds, one of which includes a putative redox-active site with the sequence CXXXC. We confirmed the importance of these cysteine residues for PmScsBα function, and in addition, we engineered cysteine variants that produced a stable complex between PmScsC and PmScsBα. Using small-angle X-ray and neutron scattering analyses with contrast variation, we determined a low-resolution structure of the PmScsC-PmScsBα c...Continue Reading

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Citations

Jan 22, 2019·Critical Reviews in Microbiology·Signe ChristensenWilhelmina M Huston
Apr 6, 2019·Acta Crystallographica. Section D, Structural Biology·Patricia M WaldenJennifer L Martin
Aug 25, 2019·The Journal of Biological Chemistry·Pramod SubediBegoña Heras
Apr 22, 2018·The Journal of Biological Chemistry·David C Goldstone, Edward N Baker
Apr 20, 2020·Journal of Molecular Biology·John H Bushweller

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