Ca2+-induced linker transformation leads to a compact and rigid collagen-binding domain of Clostridium histolyticum collagenase.

ABSTRACT: Clostridium histolyticum collagenase is responsible for extensive tissue destruction in gas gangrene, and its activity is enhanced by calcium ions. The collagen-binding domain is the minimal segment of the enzyme required for binding to insoluble collagen fibrils and for subsequent collagenolysis. The collagen-binding domain is joined to another binding module by a conserved 14-amino-acid linker. The linker undergoes secondary structural transformation from an alpha-helix to a beta-strand and forms a nonprolyl cis-peptide in the presence of calcium ions. In this study, various biophysical methods were utilized to better understand the structure and functional role of the novel calcium-activated linker. Two Ca(2+) ions bind cooperatively with macroscopic association constants of K(1) = 5.01

SUBMITTER: Philominathan ST 

PROVIDER: S-EPMC2782454 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature