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.

中文翻译：

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来自枯草芽孢杆菌的静止期存活蛋白 YuiC 的结构。

背景技术在厚壁菌门中发现固定相存活蛋白（Sps）具有相似的结构域组成，并且在某些情况下基因组背景，作为放线菌的复苏促进因子，但具有不同的推定肽聚糖切割结构域。结果发现来自枯草芽孢杆菌的厚壁菌门 Sps 蛋白 YuiC 的第一个结构是细胞壁肽聚糖水解酶 MltA 的剥离版本。YuiC 结构是域交换二聚体，尽管在溶液中也发现了一些单体。在五糖存在下结晶的蛋白质显示出 1,6-脱水二糖糖产物，表明 YuiC 至少在结晶过程中长时间温育时切割糖骨架形成脱水产物。