The dynamics and interactions of Scs proteins from Proteus mirabilis

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dc.contributor.authorWhitten, AEen_AU
dc.contributor.authorFurlong, Een_AU
dc.contributor.authorChoudhury, Fen_AU
dc.contributor.authorKurth, Fen_AU
dc.contributor.authorDuff, APen_AU
dc.contributor.authorMartin, Jen_AU
dc.date.accessioned2024-02-28T04:59:11Zen_AU
dc.date.available2024-02-28T04:59:11Zen_AU
dc.date.issued2021-08-14en_AU
dc.date.statistics2023-04-20en_AU
dc.description.abstractCorrect 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 Authorsen_AU
dc.identifier.articlenumberC202en_AU
dc.identifier.citationWhitten, 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/S0108767321094800en_AU
dc.identifier.conferenceenddate2021-08-21en_AU
dc.identifier.conferencenameIUCr 2021, 25th Congress of the International Union of Crystallographyen_AU
dc.identifier.conferenceplacePrague, Czech Republicen_AU
dc.identifier.conferencestartdate2021-08-14en_AU
dc.identifier.issn2053-2733en_AU
dc.identifier.issuea2en_AU
dc.identifier.journaltitleActa Crystallographica Section A : Foundations and Advancesen_AU
dc.identifier.otherMS-25-4en_AU
dc.identifier.urihttps://doi.org/doi:10.1107/S0108767321094800en_AU
dc.identifier.urihttps://apo.ansto.gov.au/handle/10238/15478en_AU
dc.identifier.volume77en_AU
dc.language.isoenen_AU
dc.publisherInternational Union of Crystallographyen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectProteinsen_AU
dc.subjectBacteriaen_AU
dc.subjectDisulfidesen_AU
dc.subjectMoleculesen_AU
dc.subjectAntibioticsen_AU
dc.titleThe dynamics and interactions of Scs proteins from Proteus mirabilisen_AU
dc.typeConference Abstracten_AU
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