1v5d

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[[Image:1v5d.jpg|left|200px]]
[[Image:1v5d.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1v5d |SIZE=350|CAPTION= <scene name='initialview01'>1v5d</scene>, resolution 1.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1v5d", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PIN:PIPERAZINE-N,N&#39;-BIS(2-ETHANESULFONIC+ACID)'>PIN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1v5d| PDB=1v5d | SCENE= }}
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|RELATEDENTRY=[[1v5c|1V5C]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v5d OCA], [http://www.ebi.ac.uk/pdbsum/1v5d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v5d RCSB]</span>
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}}
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'''The crystal structure of the active form chitosanase from Bacillus sp. K17 at pH6.4'''
'''The crystal structure of the active form chitosanase from Bacillus sp. K17 at pH6.4'''
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==About this Structure==
==About this Structure==
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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].
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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://www.ncbi.nlm.nih.gov/pubmed/15465062 15465062]
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]
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[[Category: Bacillus sp.]]
 
[[Category: Chitosanase]]
[[Category: Chitosanase]]
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[[Category: Protein complex]]
 
[[Category: Adachi, W.]]
[[Category: Adachi, W.]]
[[Category: Fukazawa, T.]]
[[Category: Fukazawa, T.]]
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[[Category: Takenaka, A.]]
[[Category: Takenaka, A.]]
[[Category: Yatsunami, R.]]
[[Category: Yatsunami, R.]]
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[[Category: chitosan degradation]]
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[[Category: Chitosan degradation]]
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[[Category: family 8]]
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[[Category: Family 8]]
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[[Category: glycosil hydrolase]]
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[[Category: Glycosil hydrolase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:05:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:19:40 2008''
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Revision as of 09:05, 3 May 2008

Template:STRUCTURE 1v5d

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

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 Page seeded by OCA on Sat May 3 12:05:56 2008

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