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Crystal Structure of the GerBC component of a Bacillus subtilis Spore Germinant Receptor

机译:枯草芽孢杆菌孢子萌发受体GerBC成分的晶体结构

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摘要

The nutrient germinant receptors (nGRs) of spores of Bacillus species are clusters of three proteins that play a critical role in triggering the germination of dormant spores in response to specific nutrient molecules. Here we report the crystal structure of the C protein of the GerB germinant receptor, so called GerBC, of Bacillus subtilis spores at 2.3 Å resolution. The GerBC protein adopts a previously uncharacterized type of protein fold consisting of three distinct domains, each of which is centered by a β sheet surrounded by multiple α helices. Secondary structure prediction and structure-based sequence alignment suggest that the GerBC structure represents the prototype for C subunits of nGRs from spores of all Bacillales and Clostridiales species and defines two highly conserved structural regions in this family of proteins. GerBC forms an interlocked dimer in the crystalline state but is predominantly monomeric in solution, pointing to the possibility that GerBC oligomerizes as a result of either high local protein concentrations or interaction with other nGR proteins in spores. Our findings provide the first structural view of the nGR subunits and a molecular framework for understanding the architecture, conservation and function of nGRs.
机译:芽孢杆菌种的营养素萌发受体(nGRs)是三种蛋白质的簇,它们在响应特定营养素分子触发休眠孢子萌发中起关键作用。在这里,我们报道了枯草芽孢杆菌孢子的GerB萌发受体(称为GerBC)C蛋白的晶体结构,分辨率为2.3。 GerBC蛋白采用以前未知的类型的蛋白折叠,该蛋白折叠由三个不同的域组成,每个域都以被多个α螺旋包围的β折叠为中心。二级结构预测和基于结构的序列比对表明,GerBC结构代表了来自所有芽孢杆菌和梭菌物种的孢子的nGRs C亚基的原型,并定义了该蛋白家族中的两个高度保守的结构区。 GerBC在结晶状态下形成互锁的二聚体,但在溶液中主要为单体,这表明GerBC可能由于高局部蛋白浓度或与孢子中其他nGR蛋白相互作用而寡聚。我们的发现提供了nGR亚基的第一个结构视图和一个分子框架,用于理解nGR的结构,保守性和功能。

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