1ed7
From Proteopedia
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SOLUTION STRUCTURE OF THE CHITIN-BINDING DOMAIN OF BACILLUS CIRCULANS WL-12 CHITINASE A1
Overview
The three-dimensional structure of the chitin-binding domain (ChBD) of, chitinase A1 (ChiA1) from a Gram-positive bacterium, Bacillus circulans, WL-12, was determined by means of multidimensional heteronuclear NMR, methods. ChiA1 is a glycosidase that hydrolyzes chitin and is composed of, an N-terminal catalytic domain, two fibronectin type III-like domains, and, C-terminal ChBD(ChiA1) (45 residues, Ala(655)-Gln(699)), which binds, specifically to insoluble chitin. ChBD(ChiA1) has a compact and globular, structure with the topology of a twisted beta-sandwich. This domain, contains two antiparallel beta-sheets, one composed of three strands and, the other of two strands. The core region formed by the hydrophobic and, aromatic residues makes the overall structure rigid and compact. The, overall topology of ChBD(ChiA1) is similar to that of the, cellulose-binding domain (CBD) of Erwinia chrysanthemi endoglucanase Z, (CBD(EGZ)). However, ChBD(ChiA1) lacks the three aromatic residues aligned, linearly and exposed to the solvent, which probably interact with, cellulose in CBDs. Therefore, the binding mechanism of a group of ChBDs, including ChBD(ChiA1) may be different from that proposed for CBDs.
About this Structure
1ED7 is a Single protein structure of sequence from Bacillus circulans. Active as Chitinase, with EC number 3.2.1.14 Full crystallographic information is available from OCA.
Reference
Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1., Ikegami T, Okada T, Hashimoto M, Seino S, Watanabe T, Shirakawa M, J Biol Chem. 2000 May 5;275(18):13654-61. PMID:10788483
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