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    Structure of the stationary phase survival protein YuiC from B.subtilis

    Quay, Doris H.X. and Cole, Ambrose R. and Cryar, A. and Thalassinos, Konstantinos and Williams, Mark A. and Bhakta, Sanjib and Keep, Nicholas H. (2015) Structure of the stationary phase survival protein YuiC from B.subtilis. BMC Structural Biology 15 (12), ISSN 1472-6807.

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    - Background: Stationary phase survival proteins (Sps) were found in Firmicutes as having analogous domain compositions, and in some cases genome context, as the resuscitation promoting factors of Actinobacteria, but with a different putative peptidoglycan cleaving domain. - Results: The first structure of a Firmicute Sps protein YuiC from B. subtilis, is found to be a stripped down version of the cell-wall peptidoglycan hydrolase MltA. The YuiC structures are of a domain swapped dimer, although some monomer is also found in solution. The protein crystallised in the presence of pentasaccharide shows a 1,6-anhydrodisaccharide sugar product, indicating that YuiC cleaves the sugar backbone to form an anhydro product at least on lengthy incubation during crystallisation. - Conclusions: The structural simplification of MltA in Sps proteins is analogous to that of the resuscitation promoting factor domains of Actinobacteria, which are stripped down versions of lysozyme and soluble lytic transglycosylase proteins.


    Item Type: Article
    Keyword(s) / Subject(s): Dormancy, Stationary Phase Survival, Peptidoglycan, Resuscitation Promoting Factors, Firmicutes
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Research Centres and Institutes: Bioinformatics, Bloomsbury Centre for (Closed), Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Nick Keep
    Date Deposited: 23 Jul 2015 09:10
    Last Modified: 02 Aug 2023 17:17


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