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J Biol Chem, Vol. 275, Issue 18, 13654-13661, May 5, 2000
Solution Structure of the Chitin-binding Domain of Bacillus
circulans WL-12 Chitinase A1*
Takahisa
Ikegami ,
Terumasa
Okada ,
Masayuki
Hashimoto§,
Shizuka
Seino§,
Takeshi
Watanabe§, and
Masahiro
Shirakawa ¶
From the Graduate School of Biological Sciences, Nara
Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara
630-0101, Japan and the § Department of Applied Biological
Chemistry, Faculty of Agriculture, Niigata University, 8050 Ikarashi-2, Niigata 950-2181, Japan
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 ChBDChiA1 (45 residues,
Ala655-Gln699), which binds specifically
to insoluble chitin. ChBDChiA1 has a compact and globular
structure with the topology of a twisted -sandwich. This domain
contains two antiparallel -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 ChBDChiA1 is similar to that of the
cellulose-binding domain (CBD) of Erwinia chrysanthemi
endoglucanase Z (CBDEGZ). However, ChBDChiA1
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 ChBDChiA1 may be different from that proposed for CBDs.
*
This work was supported by grants from the Ministry of
Education, Science and Culture of Japan (to M. S. and T. I.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The atomic coordinates and the structure factors (code 1ed7) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
¶
To whom correspondence should be addressed. Fax:
81-743-72-5579; Tel.: 81-743-72-5571; E-mail:
shira@bs.aist-nara.ac.jp.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
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