1wvu
From Proteopedia
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Crystal structure of chitinase C from Streptomyces griseus HUT6037
Overview
Chitinase C (ChiC) from Streptomyces griseus HUT6037 was the first, glycoside hydrolase family 19 chitinase that was found in an organism, other than higher plants. An N-terminal chitin-binding domain and a, C-terminal catalytic domain connected by a linker peptide constitute ChiC., We determined the crystal structure of full-length ChiC, which is the only, representative of the two-domain chitinases in the family. The catalytic, domain has an alpha-helix-rich fold with a deep cleft containing a, catalytic site, and lacks three loops on the domain surface compared with, the catalytic domain of plant chitinases. The chitin-binding domain is an, all-beta protein with two tryptophan residues (Trp59 and Trp60) aligned on, the surface. We suggest the binding mechanism of tri-N-acetylchitotriose, onto the chitin-binding domain on the basis of molecular dynamics (MD), simulations. In this mechanism, the ligand molecule binds well on the, surface-exposed binding site through two stacking interactions and two, hydrogen bonds and only Trp59 and Trp60 are involved in the binding., Furthermore, the flexibility of the Trp60 side-chain, which may be, involved in adjusting the binding surface to fit the surface of, crystalline chitin by the rotation of chi2 angle, is shown.
About this Structure
1WVU is a Single protein structure of sequence from Streptomyces chryseus with CL as ligand. Active as Chitinase, with EC number 3.2.1.14 Full crystallographic information is available from OCA.
Reference
Structural studies of a two-domain chitinase from Streptomyces griseus HUT6037., Kezuka Y, Ohishi M, Itoh Y, Watanabe J, Mitsutomi M, Watanabe T, Nonaka T, J Mol Biol. 2006 Apr 28;358(2):472-84. Epub 2006 Feb 21. PMID:16516924
Page seeded by OCA on Sun Nov 25 00:51:39 2007
