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Structural Basis for Activity Regulation and Substrate Preference of Clostridial Collagenases G, H, and T

24 May 2013

Abstract excerpt

Clostridial collagenases are among the most efficient enzymes to degrade by far the most predominant protein in the biosphere. Here we present crystal structures of the peptidases of three clostridial collagenase isoforms (ColG, ColH, and ColT). The comparison of unliganded and liganded structures reveals a quaternary subdomain dynamics. In the unliganded ColH structure, this globular dynamics is modulated by an...

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PMID: 23703618
DOI: 10.1074/jbc.m112.448548

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