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首页> 外文期刊>Journal of Molecular Biology >The Structure of Mycobacterium tuberculosis MPT51 (FbpC1) Defines a New Family of Non-catalytic alpha/beta Hydrolases.
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The Structure of Mycobacterium tuberculosis MPT51 (FbpC1) Defines a New Family of Non-catalytic alpha/beta Hydrolases.

机译：结核分枝杆菌MPT51（FbpC1）的结构定义了一个新的非催化α/β水解酶家族。

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摘要

Mycobacterium tuberculosis, the causative agent of tuberculosis, is known to secrete a number of highly immunogenic proteins that are thought to confer pathogenicity, in part, by mediating binding to host tissues. Among these secreted proteins are the trimeric antigen 85 (Ag85) complex and the related MPT51 protein, also known as FbpC1. While the physiological function of Ag85, a mycolyltransferase required for the biosynthesis of the cell wall component alpha,alpha'-trehalose dimycolate (or cord factor), has been identified recently, the function of the closely related MPT51 ( approximately 40% identity with the Ag85 components) remains to be established. The crystal structure of M.tuberculosis MPT51, determined to 1.7A resolution, shows that MPT51, like the Ag85 components Ag85B and Ag85C2, folds as an alpha/beta hydrolase, but it does not contain any of the catalytic elements required for mycolyltransferase activity. Moreover, the absence of a recognizable alpha,alpha'-trehalose monomycolate-bindingsite and the failure to detect an active site suggest that the function of MPT51 is of a non-enzymatic nature and that MPT51 may in fact represent a new family of non-catalytic alpha/beta hydrolases. Previous experimental evidence and the structural similarity to some integrins and carbohydrate-binding proteins led to the hypothesis that MPT51 might have a role in host tissue attachment, whereby ligands may include the serum protein fibronectin and small sugars.
机译：已知结核分枝杆菌是结核的病原体，它会分泌许多高度免疫原性的蛋白质，这些蛋白质被认为部分通过介导与宿主组织的结合而具有致病性。这些分泌的蛋白质中有三聚体抗原85（Ag85）复合物和相关的MPT51蛋白，也称为FbpC1。虽然最近已经确定了Ag85的生理功能，这是细胞壁成分α，α'-海藻糖二甲酸酯（或脐带因子）生物合成所需的霉菌基转移酶，但密切相关的MPT51的功能（与MPT51大约40％的同一性Ag85组件）仍有待建立。确定为1.7A分辨率的结核分枝杆菌MPT51的晶体结构表明，MPT51与Ag85组分Ag85B和Ag85C2一样，可以折叠为α/β水解酶，但不包含任何霉菌基转移酶活性所需的催化元素。此外，由于缺乏可识别的α，α'-海藻糖单霉酸酯结合位点，且未能检测到活性位点，表明MPT51的功能具有非酶性质，并且MPT51实际上可能代表了一个新的催化α/β水解酶。先前的实验证据以及与某些整联蛋白和碳水化合物结合蛋白的结构相似性导致以下假设：MPT51可能在宿主组织附着中起作用，从而使配体包括血清蛋白纤连蛋白和小糖。

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