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首页> 外文期刊>Biological chemistry >Polycystic kidney disease-like domains of clostridial collagenases and their role in collagen recruitment.
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Polycystic kidney disease-like domains of clostridial collagenases and their role in collagen recruitment.

机译：梭菌胶原酶的多囊肾病样结构域及其在胶原募集中的作用。

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摘要

Bacterial collagenases exhibit a multimodular domain organization. While the N-terminal collagenase unit harbors the catalytic zinc and suffices to degrade peptidic substrates, collagen substrates come in different types, explaining the requirement for accessory domains such as polycystic kidney disease (PKD)-like domains for efficient catalysis. How the recognition and unfolding of (micro-)fibrillar or triple-helical collagen is accomplished are only poorly understood. Here, we present the crystal structure of the PKD-like domain of collagenase G from Clostridium histolyticum. The beta-barrel structure reveals a two-tier architecture, connected by kinked hinge segments. Together with sheet extension as a generic oligomerization mechanism, this explains the cooperativity among accessory domains as well as their adaptivity to varying substrates.
机译：细菌胶原酶表现出多模块结构域组织。尽管N端胶原酶单元具有催化性锌并足以降解肽底物，但胶原底物的类型却不同，这说明需要有效的催化作用的辅助结构域，例如多囊肾疾病（PKD）类结构域。对（微）原纤维或三螺旋胶原的识别和展开是如何完成的知之甚少。在这里，我们介绍了溶组织梭状芽孢杆菌胶原酶G的PKD样域的晶体结构。 β桶结构揭示了由扭结铰链段连接的两层结构。连同片材延伸作为一种通用的低聚机制，这解释了辅助区域之间的协作性以及它们对变化的底物的适应性。

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