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

Structure of the stationary phase survival protein YuiC from B.subtilis.
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DOI:
10.1186/s12900-015-0039-z
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发表时间:
2015-07-11
影响因子:
--
通讯作者:
Keep NH
Keep NH
中科院分区:
生物4区
文献类型:
--
作者:
Quay DH;Cole AR;Cryar A;Thalassinos K;Williams MA;Bhakta S;Keep NH

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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. 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. 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. The online version of this article (doi:10.1186/s12900-015-0039-z) contains supplementary material, which is available to authorized users.
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