title: Polycystic kidney disease-like domains of clostridial collagenases and their role in collagen recruitment.
abstract: 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 β-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.
authors.affiliation: Division of Structural Biology, Department of Molecular Biology, University of Salzburg, Billrothstraße 11, A-5020 Salzburg, Austria.
authors.forename: Ulrich
authors.initials: U
authors.lastname: Eckhard
authors.forename: Hans
authors.initials: H
authors.lastname: Brandstetter
mesh_terms: D000595:Amino Acid Sequence; D047009:Hathewaya histolytica / Q000737:chemistry / Q000201:enzymology*; D003094:Collagen / Q000378:metabolism*; D017364:Collagenases / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D003094:Collagen; D017364:Collagenases