1wvu
From Proteopedia
(New page: 200px<br /><applet load="1wvu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wvu, resolution 2.45Å" /> '''Crystal structure of...) |
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| - | [[Image:1wvu.gif|left|200px]]<br /><applet load="1wvu" size=" | + | [[Image:1wvu.gif|left|200px]]<br /><applet load="1wvu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wvu, resolution 2.45Å" /> | caption="1wvu, resolution 2.45Å" /> | ||
'''Crystal structure of chitinase C from Streptomyces griseus HUT6037'''<br /> | '''Crystal structure of chitinase C from Streptomyces griseus HUT6037'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Chitinase C (ChiC) from Streptomyces griseus HUT6037 was the first | + | Chitinase C (ChiC) from Streptomyces griseus HUT6037 was the first glycoside hydrolase family 19 chitinase that was found in an organism other than higher plants. An N-terminal chitin-binding domain and a C-terminal catalytic domain connected by a linker peptide constitute ChiC. We determined the crystal structure of full-length ChiC, which is the only representative of the two-domain chitinases in the family. The catalytic domain has an alpha-helix-rich fold with a deep cleft containing a catalytic site, and lacks three loops on the domain surface compared with the catalytic domain of plant chitinases. The chitin-binding domain is an all-beta protein with two tryptophan residues (Trp59 and Trp60) aligned on the surface. We suggest the binding mechanism of tri-N-acetylchitotriose onto the chitin-binding domain on the basis of molecular dynamics (MD) simulations. In this mechanism, the ligand molecule binds well on the surface-exposed binding site through two stacking interactions and two hydrogen bonds and only Trp59 and Trp60 are involved in the binding. Furthermore, the flexibility of the Trp60 side-chain, which may be involved in adjusting the binding surface to fit the surface of crystalline chitin by the rotation of chi2 angle, is shown. |
==About this Structure== | ==About this Structure== | ||
| - | 1WVU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_chryseus Streptomyces chryseus] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] Full crystallographic information is available from [http:// | + | 1WVU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_chryseus Streptomyces chryseus] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: whole structure]] | [[Category: whole structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:39 2008'' |
Revision as of 13:48, 21 February 2008
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Crystal structure of chitinase C from Streptomyces griseus HUT6037
Overview
Chitinase C (ChiC) from Streptomyces griseus HUT6037 was the first glycoside hydrolase family 19 chitinase that was found in an organism other than higher plants. An N-terminal chitin-binding domain and a C-terminal catalytic domain connected by a linker peptide constitute ChiC. We determined the crystal structure of full-length ChiC, which is the only representative of the two-domain chitinases in the family. The catalytic domain has an alpha-helix-rich fold with a deep cleft containing a catalytic site, and lacks three loops on the domain surface compared with the catalytic domain of plant chitinases. The chitin-binding domain is an all-beta protein with two tryptophan residues (Trp59 and Trp60) aligned on the surface. We suggest the binding mechanism of tri-N-acetylchitotriose onto the chitin-binding domain on the basis of molecular dynamics (MD) simulations. In this mechanism, the ligand molecule binds well on the surface-exposed binding site through two stacking interactions and two hydrogen bonds and only Trp59 and Trp60 are involved in the binding. Furthermore, the flexibility of the Trp60 side-chain, which may be involved in adjusting the binding surface to fit the surface of crystalline chitin by the rotation of chi2 angle, is shown.
About this Structure
1WVU is a Single protein structure of sequence from Streptomyces chryseus with as ligand. Active as Chitinase, with EC number 3.2.1.14 Full crystallographic information is available from OCA.
Reference
Structural studies of a two-domain chitinase from Streptomyces griseus HUT6037., Kezuka Y, Ohishi M, Itoh Y, Watanabe J, Mitsutomi M, Watanabe T, Nonaka T, J Mol Biol. 2006 Apr 28;358(2):472-84. Epub 2006 Feb 21. PMID:16516924
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