Ontology highlight
ABSTRACT:
SUBMITTER: Wilson JJ
PROVIDER: S-EPMC154464 | biostudies-literature | 2003 Apr
REPOSITORIES: biostudies-literature
Wilson Jeffrey J JJ Matsushita Osamu O Okabe Akinobu A Sakon Joshua J
The EMBO journal 20030401 8
The crystal structure of a collagen-binding domain (CBD) with an N-terminal domain linker from Clostridium histolyticum class I collagenase was determined at 1.00 A resolution in the absence of calcium (1NQJ) and at 1.65 A resolution in the presence of calcium (1NQD). The mature enzyme is composed of four domains: a metalloprotease domain, a spacing domain and two CBDs. A 12-residue-long linker is found at the N-terminus of each CBD. In the absence of calcium, the CBD reveals a beta-sheet sandwi ...[more]