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BioMed Central, BMC Structural Biology, 1(15), 2015

DOI: 10.1186/s12900-015-0039-z

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

Journal article published in 2015 by Doris H. X. Quay, Ambrose R. Cole, Adam Cryar, Konstantinos Thalassinos, Mark A. Williams ORCID, Sanjib Bhakta, Nicholas H. Keep
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Abstract 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.