1v5d
From Proteopedia
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| - | [[Image:1v5d.jpg|left|200px]] | + | [[Image:1v5d.jpg|left|200px]] |
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| - | '''The crystal structure of the active form chitosanase from Bacillus sp. K17 at pH6.4''' | + | {{Structure |
| + | |PDB= 1v5d |SIZE=350|CAPTION= <scene name='initialview01'>1v5d</scene>, resolution 1.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PIN:PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID)'>PIN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Chitosanase Chitosanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.132 3.2.1.132] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''The crystal structure of the active form chitosanase from Bacillus sp. K17 at pH6.4''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1V5D is a [ | + | 1V5D is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V5D OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of family GH-8 chitosanase with subclass II specificity from Bacillus sp. K17., Adachi W, Sakihama Y, Shimizu S, Sunami T, Fukazawa T, Suzuki M, Yatsunami R, Nakamura S, Takenaka A, J Mol Biol. 2004 Oct 22;343(3):785-95. PMID:[http:// | + | Crystal structure of family GH-8 chitosanase with subclass II specificity from Bacillus sp. K17., Adachi W, Sakihama Y, Shimizu S, Sunami T, Fukazawa T, Suzuki M, Yatsunami R, Nakamura S, Takenaka A, J Mol Biol. 2004 Oct 22;343(3):785-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15465062 15465062] |
[[Category: Bacillus sp.]] | [[Category: Bacillus sp.]] | ||
[[Category: Chitosanase]] | [[Category: Chitosanase]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:41:03 2008'' |
Revision as of 12:41, 20 March 2008
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| , resolution 1.50Å | |||||||
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| Ligands: | |||||||
| Activity: | Chitosanase, with EC number 3.2.1.132 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of the active form chitosanase from Bacillus sp. K17 at pH6.4
Overview
Crystal structures of chitosanase from Bacillus sp. K17 (ChoK) have been determined at 1.5 A resolution in the active form and at 2.0 A resolution in the inactive form. This enzyme belongs to the family GH-8, out of 93 glycoside hydrolase families, and exhibits the substrate specificity of subclass II chitosanase. The catalytic site is constructed on the scaffold of a double-alpha(6)/alpha(6)-barrel, which is formed by six repeating helix-loop-helix motifs. This structure is quite different from those of the GH-46 chitosanases and of GH-5. Structural comparison with CelA (a cellulase belonging to the same family GH-8) suggests that the proton donor Glu122 is conserved, but the proton acceptor is the inserted Glu309 residue, and that the corresponding Asp278 residue in CelA is inactivated in ChoK. The four acidic residues, Asp179, Glu309, Asp183 and Glu107, can be involved in substrate recognition through interactions with the amino groups of the glucosamine residues bound in the -3, -2, -1 and +1 sites, respectively. The hydrophobic Trp235, Trp166, Phe413 and Tyr318 residues are highly conserved for binding of the hexose rings at the -3, -2, +1 and +2 sites, respectively. These structural features indicate that enzymes in GH-8 can be further divided into three subfamilies. Different types of chitosanases are discussed in terms of convergent evolution from different structural ancestors.
About this Structure
1V5D is a Protein complex structure of sequences from Bacillus sp.. Full crystallographic information is available from OCA.
Reference
Crystal structure of family GH-8 chitosanase with subclass II specificity from Bacillus sp. K17., Adachi W, Sakihama Y, Shimizu S, Sunami T, Fukazawa T, Suzuki M, Yatsunami R, Nakamura S, Takenaka A, J Mol Biol. 2004 Oct 22;343(3):785-95. PMID:15465062
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