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Journal of Biochemistry 2006 139(3):483-493; doi:10.1093/jb/mvj062
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© 2006 The Japanese Biochemical Society.

Regular Paper

Identification of the Substrate Interaction Region of the Chitin-Binding Domain of Streptomyces griseus Chitinase C

Ken-ichi Akagi1, Jun Watanabe2, Masashi Hara2, Yuichiro Kezuka3, Eriko Chikaishi1, Tohru Yamaguchi4, Hideo Akutsu1, Takamasa Nonaka3, Takeshi Watanabe2 and Takahisa Ikegami1,*

1 Laboratory of Structural Proteomics, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871; 2 Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, 8050 Ikarashi-2, Niigata 950-2181; 3 Department of BioEngineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188; and 4 Discovery Research Laboratories, Shionogi & Co., Ltd., 12-4, Sagisu 5, Fukushima, Osaka 553-0002

* To whom correspondence should be addressed. Tel: +81-6-6879-8598, Fax: +81-6-6879-8599, E-mail: tiik{at}protein.osaka-u.ac.jp

Chitinase C from Streptomyces griseus HUT6037 was discovered as the first bacterial chitinase in family 19 other than chitinases found in higher plants. Chitinase C comprises two domains: a chitin-binding domain (ChBDChiC) for attachment to chitin and a chitin-catalytic domain for digesting chitin. The structure of ChBDChiC was determined by means of 13C-, 15N-, and 1H-resonance nuclear magnetic resonance (NMR) spectroscopy. The conformation of its backbone comprised two ß-sheets composed of two and three antiparallel ß-strands, respectively, this being very similar to the backbone conformations of the cellulose-binding domain of endoglucanase Z from Erwinia chrysanthemi (CBDEGZ) and the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12 (ChBDChiA1). The interaction between ChBDChiC and hexa-N-acetyl-chitohexaose was monitored through chemical shift perturbations, which showed that ChBDChiC interacted with the substrate through two aromatic rings exposed to the solvent as CBDEGZ interacts with cellulose through three characteristic aromatic rings. Comparison of the conformations of ChBDChiA1, ChBDChiC, and other typical chitin- and cellulose-binding domains, which have three solvent-exposed aromatic residues responsible for binding to polysaccharides, has suggested that they have adopted versatile binding site conformations depending on the substrates, with almost the same backbone conformations being retained.


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