The dynamics and interactions of Scs proteins from Proteus mirabilis
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Date
2021-08-14
Journal Title
Journal ISSN
Volume Title
Publisher
International Union of Crystallography
Abstract
Correct formation of disulfide bonds is critical to the folding of a wide variety of proteins. Bacterial virulence factors are one class of proteins containing disulfide bonds, thus, an approach to disarm virulent bacterial might involve shutting down the machinery involved in the formation of disulfide bonds. The suppressor of copper sensitivity (Scs) proteins form part of the disulfide bond forming machinery in bacteria, and it is hoped that determining the structure of molecules such as this may lead to the development of new classes of antibiotics. There are four Scs proteins (ScsA, B, C and D) present in numerous Gram-negative bacteria, and few have been structurally characterised. In this work we show that the ScsC protein from Proteus mirabilis is trimeric and flexible, where the high level of flexibility is afforded by a glutamine rich motif. We also show that the protein interacts with ScsB and that this interaction rigidifies the ScsC protein © The Authors
Description
Keywords
Small angle scattering, Proteins, Bacteria, Disulfides, Molecules, Antibiotics
Citation
Whitten, A., Furlong, E., Choudhury, H., Kurth, F., Duff, A., & Martin, J. (2021). The dynamics and interactions of Scs proteins from Proteus mirabilis. Paper presented to the IUCr 2021, 25th Congress of the International Union of Crystallography, 14-22 August 2021, Prague, Czech Republic. In Acta Crystallographica Section A : Foundations and Advances, 77(a2), C202. doi:10.1107/S0108767321094800