Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ikegami, T.
Right arrow Articles by Shirakawa, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ikegami, T.
Right arrow Articles by Shirakawa, M.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

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 IkegamiDagger , Terumasa OkadaDagger , Masayuki Hashimoto§, Shizuka Seino§, Takeshi Watanabe§, and Masahiro ShirakawaDagger

From the Dagger  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 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 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.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Proc. Natl. Acad. Sci. USAHome page
S. DebRoy, J. Dao, M. Soderberg, O. Rossier, and N. P. Cianciotto
Legionella pneumophila type II secretome reveals unique exoproteins and a chitinase that promotes bacterial persistence in the lung
PNAS, December 12, 2006; 103(50): 19146 - 19151.
[Abstract] [Full Text] [PDF]


Home page
J BiochemHome page
K.-i. Akagi, J. Watanabe, M. Hara, Y. Kezuka, E. Chikaishi, T. Yamaguchi, H. Akutsu, T. Nonaka, T. Watanabe, and T. Ikegami
Identification of the Substrate Interaction Region of the Chitin-Binding Domain of Streptomyces griseus Chitinase C.
J. Biochem., March 1, 2006; 139(3): 483 - 493.
[Abstract] [Full Text] [PDF]


Home page
Appl. Environ. Microbiol.Home page
Q. Li, F. Wang, Y. Zhou, and X. Xiao
Putative Exposed Aromatic and Hydroxyl Residues on the Surface of the N-Terminal Domains of Chi1 from Aeromonas caviae CB101 Are Essential for Chitin Binding and Hydrolysis
Appl. Envir. Microbiol., November 1, 2005; 71(11): 7559 - 7561.
[Abstract] [Full Text] [PDF]


Home page
Appl. Environ. Microbiol.Home page
P. A. Colussi, C. A. Specht, and C. H. Taron
Characterization of a Nucleus-Encoded Chitinase from the Yeast Kluyveromyces lactis
Appl. Envir. Microbiol., June 1, 2005; 71(6): 2862 - 2869.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
A. Fokine, P. G. Leiman, M. M. Shneider, B. Ahvazi, K. M. Boeshans, A. C. Steven, L. W. Black, V. V. Mesyanzhinov, and M. G. Rossmann
Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry
PNAS, May 17, 2005; 102(20): 7163 - 7168.
[Abstract] [Full Text] [PDF]


Home page
GENES CELLSHome page
T. Tenno, K. Fujiwara, H. Tochio, K. Iwai, E. H. Morita, H. Hayashi, S. Murata, H. Hiroaki, M. Sato, K. Tanaka, et al.
Structural basis for distinct roles of Lys63- and Lys48-linked polyubiquitin chains
Genes Cells, October 1, 2004; 9(10): 865 - 875.
[Abstract] [Full Text] [PDF]


Home page
Appl. Environ. Microbiol.Home page
D. Y. Kobayashi, R. M. Reedy, J. Bick, and P. V. Oudemans
Characterization of a Chitinase Gene from Stenotrophomonas maltophilia Strain 34S1 and Its Involvement in Biological Control
Appl. Envir. Microbiol., March 1, 2002; 68(3): 1047 - 1054.
[Abstract] [Full Text] [PDF]


Home page
Appl. Environ. Microbiol.Home page
M. L. Wu, Y. C. Chuang, J. P. Chen, C. S. Chen, and M. C. Chang
Identification and Characterization of the Three Chitin-Binding Domains within the Multidomain Chitinase Chi92 from Aeromonas hydrophila JP101
Appl. Envir. Microbiol., November 1, 2001; 67(11): 5100 - 5106.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
T. Uchiyama, F. Katouno, N. Nikaidou, T. Nonaka, J. Sugiyama, and T. Watanabe
Roles of the Exposed Aromatic Residues in Crystalline Chitin Hydrolysis by Chitinase A from Serratia marcescens 2170
J. Biol. Chem., October 26, 2001; 276(44): 41343 - 41349.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J.-G. Jee, T. Ikegami, M. Hashimoto, T. Kawabata, M. Ikeguchi, T. Watanabe, and M. Shirakawa
Solution Structure of the Fibronectin Type III Domain from Bacillus circulans WL-12 Chitinase A1
J. Biol. Chem., January 4, 2002; 277(2): 1388 - 1397.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement