1h8v

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==Overview==
==Overview==
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We present the three-dimensional structure of Trichoderma reesei, endoglucanase 3 (Cel12A), a small, 218 amino acid residue (24.5 kDa), neutral pI, glycoside hydrolase family 12 cellulase that lacks a, cellulose-binding module. The structure has been determined using X-ray, crystallography and refined to 1.9 A resolution. The asymmetric unit, consists of six non-crystallographic symmetry-related molecules that were, exploited to improve initial multiple isomorphous replacement phasing, and, subsequent structure refinement. The enzyme contains one disulfide bridge, and is glycosylated at Asp164 by a single N-acetyl glucosamine residue., The protein has the expected fold for a glycoside hydrolase clan-C family, 12 enzyme. It contains two beta-sheets, of six and nine strands, packed on, top of one another, and one alpha-helix. The concave surface of the, nine-stranded beta-sheet forms a large substrate-binding groove in which, the active-site residues are located. In the active site, we find a, carboxylic acid trio, similar to that of glycoside hydrolase families 7, and 16. The strictly conserved Asp99 hydrogen bonds to the nucleophile, the invariant Glu116. The binding crevice is lined with both aromatic and, polar amino acid side-chains which may play a role in substrate binding., The structure of the fungal family 12 enzyme presented here allows a, complete structural characterization of the glycoside hydrolase-C clan.
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We present the three-dimensional structure of Trichoderma reesei endoglucanase 3 (Cel12A), a small, 218 amino acid residue (24.5 kDa), neutral pI, glycoside hydrolase family 12 cellulase that lacks a cellulose-binding module. The structure has been determined using X-ray crystallography and refined to 1.9 A resolution. The asymmetric unit consists of six non-crystallographic symmetry-related molecules that were exploited to improve initial multiple isomorphous replacement phasing, and subsequent structure refinement. The enzyme contains one disulfide bridge and is glycosylated at Asp164 by a single N-acetyl glucosamine residue. The protein has the expected fold for a glycoside hydrolase clan-C family 12 enzyme. It contains two beta-sheets, of six and nine strands, packed on top of one another, and one alpha-helix. The concave surface of the nine-stranded beta-sheet forms a large substrate-binding groove in which the active-site residues are located. In the active site, we find a carboxylic acid trio, similar to that of glycoside hydrolase families 7 and 16. The strictly conserved Asp99 hydrogen bonds to the nucleophile, the invariant Glu116. The binding crevice is lined with both aromatic and polar amino acid side-chains which may play a role in substrate binding. The structure of the fungal family 12 enzyme presented here allows a complete structural characterization of the glycoside hydrolase-C clan.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bott, R.]]
[[Category: Bott, R.]]
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[[Category: Cameron, A.D.]]
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[[Category: Cameron, A D.]]
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[[Category: Jones, T.A.]]
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[[Category: Jones, T A.]]
[[Category: Mitchinson, C.]]
[[Category: Mitchinson, C.]]
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[[Category: Ropp, T.H.]]
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[[Category: Ropp, T H.]]
[[Category: Sandgren, M.]]
[[Category: Sandgren, M.]]
[[Category: Shaw, A.]]
[[Category: Shaw, A.]]
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[[Category: trichoderma reesei cel12a]]
[[Category: trichoderma reesei cel12a]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:47:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:42 2008''

Revision as of 10:58, 21 February 2008


1h8v, resolution 1.90Å

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THE X-RAY CRYSTAL STRUCTURE OF THE TRICHODERMA REESEI FAMILY 12 ENDOGLUCANASE 3, CEL12A, AT 1.9 A RESOLUTION

Overview

We present the three-dimensional structure of Trichoderma reesei endoglucanase 3 (Cel12A), a small, 218 amino acid residue (24.5 kDa), neutral pI, glycoside hydrolase family 12 cellulase that lacks a cellulose-binding module. The structure has been determined using X-ray crystallography and refined to 1.9 A resolution. The asymmetric unit consists of six non-crystallographic symmetry-related molecules that were exploited to improve initial multiple isomorphous replacement phasing, and subsequent structure refinement. The enzyme contains one disulfide bridge and is glycosylated at Asp164 by a single N-acetyl glucosamine residue. The protein has the expected fold for a glycoside hydrolase clan-C family 12 enzyme. It contains two beta-sheets, of six and nine strands, packed on top of one another, and one alpha-helix. The concave surface of the nine-stranded beta-sheet forms a large substrate-binding groove in which the active-site residues are located. In the active site, we find a carboxylic acid trio, similar to that of glycoside hydrolase families 7 and 16. The strictly conserved Asp99 hydrogen bonds to the nucleophile, the invariant Glu116. The binding crevice is lined with both aromatic and polar amino acid side-chains which may play a role in substrate binding. The structure of the fungal family 12 enzyme presented here allows a complete structural characterization of the glycoside hydrolase-C clan.

About this Structure

1H8V is a Single protein structure of sequence from Hypocrea jecorina with as ligand. Active as Cellulase, with EC number 3.2.1.4 Known structural/functional Sites: , , , , and . Full crystallographic information is available from OCA.

Reference

The X-ray crystal structure of the Trichoderma reesei family 12 endoglucanase 3, Cel12A, at 1.9 A resolution., Sandgren M, Shaw A, Ropp TH, Wu S, Bott R, Cameron AD, Stahlberg J, Mitchinson C, Jones TA, J Mol Biol. 2001 Apr 27;308(2):295-310. PMID:11327768

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