1nqd
From Proteopedia
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CRYSTAL STRUCTURE OF CLOSTRIDIUM HISTOLYTICUM COLG COLLAGENASE COLLAGEN-BINDING DOMAIN 3B AT 1.65 ANGSTROM RESOLUTION IN PRESENCE OF CALCIUM
Overview
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.
About this Structure
1NQD is a Single protein structure of sequence from Clostridium histolyticum with CA as ligand. Active as Microbial collagenase, with EC number 3.4.24.3 Full crystallographic information is available from OCA.
Reference
A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation., Wilson JJ, Matsushita O, Okabe A, Sakon J, EMBO J. 2003 Apr 15;22(8):1743-52. PMID:12682007
Page seeded by OCA on Sat Nov 24 23:34:41 2007
