Polycystic kidney disease-like domains of clostridial collagenases and their role in collagen recruitment

Ulrich Eckhard, Hans Brandstetter

    Publikation: Beitrag in FachzeitschriftArtikel

    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.

    OriginalspracheEnglisch
    Seiten (von - bis)1039-45
    Seitenumfang7
    FachzeitschriftBiological Chemistry
    Jahrgang392
    Ausgabenummer11
    DOIs
    PublikationsstatusVeröffentlicht - Nov 2011

    Systematik der Wissenschaftszweige 2012

    • 106 Biologie

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