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

IF 2.222 Q3 Biochemistry, Genetics and Molecular Biology

BMC Structural Biology Pub Date : 2015-07-11 DOI:10.1186/s12900-015-0039-z

Doris H.X. Quay, Ambrose R. Cole, Adam Cryar, Konstantinos Thalassinos, Mark A. Williams, Sanjib Bhakta, Nicholas H. Keep

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引用次数: 9

Abstract

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.

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枯草芽孢杆菌固定相存活蛋白YuiC的结构研究

在厚壁菌门中发现固定相存活蛋白(Sps)具有类似的结构域组成，在某些情况下，作为放线菌门的复苏促进因子，但具有不同的肽聚糖切割结构域。来自枯草芽孢杆菌的厚壁菌Sps蛋白YuiC的第一个结构被发现是细胞壁肽聚糖水解酶MltA的剥离版本。YuiC结构是一个交换的二聚体，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为1,6-无水双糖糖产物，表明YuiC在结晶过程中至少在长时间的孵育过程中裂解糖骨架形成无水产物。Sps蛋白中MltA的结构简化类似于放线菌的复苏促进因子结构域，这是溶菌酶和可溶性水解转糖基酶蛋白的剥离版本。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

BMC Structural Biology 生物-生物物理

CiteScore

3.60

自引率

0.00%

发文量

期刊介绍： BMC Structural Biology is an open access, peer-reviewed journal that considers articles on investigations into the structure of biological macromolecules, including solving structures, structural and functional analyses, and computational modeling.