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1h8v
From Proteopedia
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| - | [[Image:1h8v.jpg|left|200px]] | + | [[Image:1h8v.jpg|left|200px]] |
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| - | '''THE X-RAY CRYSTAL STRUCTURE OF THE TRICHODERMA REESEI FAMILY 12 ENDOGLUCANASE 3, CEL12A, AT 1.9 A RESOLUTION''' | + | {{Structure |
| + | |PDB= 1h8v |SIZE=350|CAPTION= <scene name='initialview01'>1h8v</scene>, resolution 1.90Å | ||
| + | |SITE= <scene name='pdbsite=CA1:The+Active-Site+Residues+That+Are+Involve+In+Catalysis+A+...'>CA1</scene>, <scene name='pdbsite=CA2:The+Active-Site+Residues+That+Are+Involve+In+Catalysis+A+...'>CA2</scene>, <scene name='pdbsite=CA3:The+Active-Site+Residues+That+Are+Involve+In+Catalysis+A+...'>CA3</scene>, <scene name='pdbsite=CA4:The+Active-Site+Residues+That+Are+Involve+In+Catalysis+A+...'>CA4</scene>, <scene name='pdbsite=CA5:The+Active-Site+Residues+That+Are+Involve+In+Catalysis+A+...'>CA5</scene> and <scene name='pdbsite=CA6:The+Active-Site+Residues+That+Are+Involve+In+Catalysis+A+...'>CA6</scene> | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE X-RAY CRYSTAL STRUCTURE OF THE TRICHODERMA REESEI FAMILY 12 ENDOGLUCANASE 3, CEL12A, AT 1.9 A RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H8V is a [ | + | 1H8V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8V OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11327768 11327768] |
[[Category: Cellulase]] | [[Category: Cellulase]] | ||
[[Category: Hypocrea jecorina]] | [[Category: Hypocrea jecorina]] | ||
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[[Category: trichoderma reesei cel12a]] | [[Category: trichoderma reesei cel12a]] | ||
| - | ''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 11:33:50 2008'' |
Revision as of 09:33, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Sites: | , , , , and | ||||||
| Ligands: | |||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 11:33:50 2008
Categories: Cellulase | Hypocrea jecorina | Single protein | Bott, R. | Cameron, A D. | Jones, T A. | Mitchinson, C. | Ropp, T H. | Sandgren, M. | Shaw, A. | Stahlberg, J. | Wu, S. | NAG | Cellulose degradation | Endoglucanase | Gh family 12 | Glycosyl hydrolase | Hydrolase | Trichoderma reesei cel12a
