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首页> 外文期刊>Journal of Molecular Biology >Three-dimensional structure of a putative non-cellulosomal cohesin module from a Clostridium perfringens family 84 glycoside hydrolase
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Three-dimensional structure of a putative non-cellulosomal cohesin module from a Clostridium perfringens family 84 glycoside hydrolase

机译：产气荚膜梭菌家族84糖苷水解酶推定的非纤维素黏附素模块的三维结构

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The genomes of myonecrotic strains of Clostridium perftingens encode a large number of secreted glycoside hydrolases. The activities of these enzymes are consistent with degradation of the mucosal layer of the human gastrointestinal tract, glycosaminoglycans and other cellular glycans found throughout the body. In many cases this is thought to aid in the propagation of the major toxins produced by C. perftingens. One such example is the family 84 glycoside hydrolases, which contains five C. perfringens members (CpGH84A-E), each displaying a unique modular architecture. The smallest and most extensively studied member, CpGH84C, comprises an N-terminal catalytic domain with beta-N-acetylglucosaminidase activity, a family 32 carbohydrate-binding module, a family 82 X-module (X82) of unknown function, and a fibronectin type-III-like module. Here we present the structure of the X82 module from CpGH84C, determined by both NMR spectroscopy and X-ray crystallography. CpGH84C X82 adopts a jell-roll fold comprising two beta-sheets formed by nine beta-strands. CpGH84C X82 displays distant amino acid sequence identity yet close structural similarity to the cohesin modules of cellulolytic anaerobic bacteria. Cohesin modules are responsible for the assembly of numerous hydrolytic enzymes m a cellulose-degrading multi-enzyme complex, termed the cellulosome, through a high-affinity interaction with the calcium-binding dockerin module. A planar surface is located on the face of the CpGH84 X82 structure that corresponds to the dockerin-binding region of cellulolytic cohesin modules and has the approximate dimensions to accommodate a dockerin module. The presence of cohesin-like X82 modules in glycoside hydrolases of C. perfringens is an indication that the formation of novel X82-dockerin mediated multi-enzyme complexes, with potential roles in pathogenesis, is possible. (c) 2007 Elsevier Ltd. All rights reserved.
机译：产气荚膜梭菌的坏死菌株的基因组编码大量分泌的糖苷水解酶。这些酶的活性与人体胃肠道粘膜层，糖胺聚糖和遍布全身的其他细胞聚糖的降解一致。在许多情况下，这被认为有助于繁殖由产气荚膜梭菌产生的主要毒素。一个这样的例子是家族84糖苷水解酶，其包含五个产气荚膜梭菌成员（CpGH84A-E），每个成员展示独特的模块化结构。最小且研究最广泛的成员CpGH84C，包括具有β-N-乙酰氨基葡萄糖苷酶活性的N末端催化域，家族32碳水化合物结合模块，未知功能的家族82 X模块（X82）和纤连蛋白类型-III类模块。在这里，我们介绍了CpGH84C的X82模块的结构，该结构通过NMR光谱学和X射线晶体学测定。 CpGH84C X82采用果冻卷式折叠，包括两个由九个β链形成的β折叠。 CpGH84C X82与纤维素分解厌氧细菌的粘附素模块显示出遥远的氨基酸序列同一性，但结构相似。粘着素模块通过与钙结合的dockerin模块之间的高亲和力相互作用，负责在纤维素降解的多酶复合物（称为纤维素体）中组装多种水解酶。平坦表面位于CpGH84 X82结构的表面上，该表面对应于纤维素分解黏着蛋白模块的dockerin结合区域，并具有近似尺寸以容纳dockerin模块。产气荚膜梭菌糖苷水解酶中黏附素样X82组件的存在表明可能形成新的X82-dockerin介导的多酶复合物，在发病机理中具有潜在作用。 （c）2007 Elsevier Ltd.保留所有权利。

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