2d49
From Proteopedia
(New page: 200px<br /><applet load="2d49" size="350" color="white" frame="true" align="right" spinBox="true" caption="2d49" /> '''Solution structure of the Chitin-Binding Dom...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Chitinase C from Streptomyces griseus HUT6037 was discovered as the first | + | 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 (ChBD(ChiC)) for attachment to chitin and a chitin-catalytic domain for digesting chitin. The structure of ChBD(ChiC) was determined by means of 13C-, 15N-, and 1H-resonance nuclear magnetic resonance (NMR) spectroscopy. The conformation of its backbone comprised two beta-sheets composed of two and three antiparallel beta-strands, respectively, this being very similar to the backbone conformations of the cellulose-binding domain of endoglucanase Z from Erwinia chrysanthemi (CBD(EGZ)) and the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12 (ChBD(ChiA1)). The interaction between ChBD(ChiC) and hexa-N-acetyl-chitohexaose was monitored through chemical shift perturbations, which showed that ChBD(ChiC) interacted with the substrate through two aromatic rings exposed to the solvent as CBD(EGZ) interacts with cellulose through three characteristic aromatic rings. Comparison of the conformations of ChBD(ChiA1), ChBD(ChiC), 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. |
==About this Structure== | ==About this Structure== | ||
| Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | Identification of the substrate interaction region of the chitin-binding domain of Streptomyces griseus chitinase C., Akagi K, Watanabe J, Hara M, Kezuka Y, Chikaishi E, Yamaguchi T, Akutsu H, Nonaka T, Watanabe T, Ikegami T, J Biochem | + | Identification of the substrate interaction region of the chitin-binding domain of Streptomyces griseus chitinase C., Akagi K, Watanabe J, Hara M, Kezuka Y, Chikaishi E, Yamaguchi T, Akutsu H, Nonaka T, Watanabe T, Ikegami T, J Biochem. 2006 Mar;139(3):483-93. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16567413 16567413] |
[[Category: Chitinase]] | [[Category: Chitinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 28: | Line 28: | ||
[[Category: chitinase]] | [[Category: chitinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:15 2008'' |
Revision as of 14:55, 21 February 2008
|
Solution structure of the Chitin-Binding Domain of Streptomyces griseus Chitinase C
Overview
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 (ChBD(ChiC)) for attachment to chitin and a chitin-catalytic domain for digesting chitin. The structure of ChBD(ChiC) was determined by means of 13C-, 15N-, and 1H-resonance nuclear magnetic resonance (NMR) spectroscopy. The conformation of its backbone comprised two beta-sheets composed of two and three antiparallel beta-strands, respectively, this being very similar to the backbone conformations of the cellulose-binding domain of endoglucanase Z from Erwinia chrysanthemi (CBD(EGZ)) and the chitin-binding domain of chitinase A1 from Bacillus circulans WL-12 (ChBD(ChiA1)). The interaction between ChBD(ChiC) and hexa-N-acetyl-chitohexaose was monitored through chemical shift perturbations, which showed that ChBD(ChiC) interacted with the substrate through two aromatic rings exposed to the solvent as CBD(EGZ) interacts with cellulose through three characteristic aromatic rings. Comparison of the conformations of ChBD(ChiA1), ChBD(ChiC), 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.
About this Structure
2D49 is a Single protein structure of sequence from Streptomyces chryseus. Active as Chitinase, with EC number 3.2.1.14 Full crystallographic information is available from OCA.
Reference
Identification of the substrate interaction region of the chitin-binding domain of Streptomyces griseus chitinase C., Akagi K, Watanabe J, Hara M, Kezuka Y, Chikaishi E, Yamaguchi T, Akutsu H, Nonaka T, Watanabe T, Ikegami T, J Biochem. 2006 Mar;139(3):483-93. PMID:16567413
Page seeded by OCA on Thu Feb 21 16:55:15 2008
