期刊
BIOLOGICAL CHEMISTRY
卷 392, 期 11, 页码 1039-1045出版社
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2011.099
关键词
calcium switch; Clostridium histolyticum; collagen binding domains; disorder-order transition; hydrophobic core; structural plasticity
资金
- Austrian Science Fund FWF [P_20582]
- Austrian Science Fund (FWF) [P 20582] Funding Source: researchfish
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.
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