1NQD

CRYSTAL STRUCTURE OF CLOSTRIDIUM HISTOLYTICUM COLG COLLAGENASE COLLAGEN-BINDING DOMAIN 3B AT 1.65 ANGSTROM RESOLUTION IN PRESENCE OF CALCIUM

Summary for 1NQD

• Entry DOI: 10.2210/pdb1nqd/pdb
• Related: 1NQJ
• Descriptor: class 1 collagenase, CALCIUM ION (3 entities in total)
• Functional Keywords: beta sandwich, metalloprotease, collagen-binding domain, calcium, hydrolase
• Biological source: Clostridium histolyticum
• Total number of polymer chains: 2
• Total formula weight: 27770.69

Authors

Wilson, J.J.,Matsushita, O.,Okabe, A.,Sakon, J. (deposition date: 2003-01-21, release date: 2003-04-15, Last modification date: 2024-04-03)

Primary citation

Wilson, J.J.,Matsushita, O.,Okabe, A.,Sakon, J.
A Bacterial Collagen-Binding Domain with Novel Calcium-Binding Motif Controls Domain Orientation
Embo J., 22:1743-1752, 2003

PubMed Abstract: 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 sandwich fold with the linker adopting an alpha-helix. The addition of calcium unwinds the linker and anchors it to the distal side of the sandwich as a new beta-strand. The conformational change of the linker upon calcium binding is confirmed by changes in the Stokes and hydrodynamic radii as measured by size exclusion chromatography and by dynamic light scattering with and without calcium. Furthermore, extensive mutagenesis of conserved surface residues and collagen-binding studies allow us to identify the collagen-binding surface of the protein and propose likely collagen-protein binding models.

PubMed: 12682007
DOI: 10.1093/emboj/cdg172

Experimental method

X-RAY DIFFRACTION (1.65 Å)