1h8v: Difference between revisions
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|PDB= 1h8v |SIZE=350|CAPTION= <scene name='initialview01'>1h8v</scene>, resolution 1.90Å | |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> | |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> | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8v OCA], [http://www.ebi.ac.uk/pdbsum/1h8v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h8v RCSB]</span> | |||
}} | }} | ||
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[[Category: Stahlberg, J.]] | [[Category: Stahlberg, J.]] | ||
[[Category: Wu, S.]] | [[Category: Wu, S.]] | ||
[[Category: cellulase]] | [[Category: cellulase]] | ||
[[Category: cellulose degradation]] | [[Category: cellulose degradation]] | ||
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[[Category: trichoderma reesei cel12a]] | [[Category: trichoderma reesei cel12a]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:00:11 2008'' | ||
Revision as of 21:00, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , and | ||||||
| Ligands: | , | ||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
OverviewOverview
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 StructureAbout this Structure
1H8V is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.
ReferenceReference
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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