1eg1: Difference between revisions
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|PDB= 1eg1 |SIZE=350|CAPTION= <scene name='initialview01'>1eg1</scene>, resolution 3.6Å | |PDB= 1eg1 |SIZE=350|CAPTION= <scene name='initialview01'>1eg1</scene>, resolution 3.6Å | ||
|SITE= | |SITE= | ||
|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=1eg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eg1 OCA], [http://www.ebi.ac.uk/pdbsum/1eg1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eg1 RCSB]</span> | |||
}} | }} | ||
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[[Category: Kleywegt, G J.]] | [[Category: Kleywegt, G J.]] | ||
[[Category: Zou, J Y.]] | [[Category: Zou, J Y.]] | ||
[[Category: cellulose degradation]] | [[Category: cellulose degradation]] | ||
[[Category: endoglucanase]] | [[Category: endoglucanase]] | ||
[[Category: mutation]] | [[Category: mutation]] | ||
''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 20:01:49 2008'' | ||
Revision as of 20:01, 30 March 2008
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| , resolution 3.6Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ENDOGLUCANASE I FROM TRICHODERMA REESEI
OverviewOverview
Cellulose is the most abundant polymer in the biosphere. Although generally resistant to degradation, it may be hydrolysed by cellulolytic organisms that have evolved a variety of structurally distinct enzymes, cellobiohydrolases and endoglucanases, for this purpose. Endoglucanase I (EG I) is the major endoglucanase produced by the cellulolytic fungus Trichoderma reesei, accounting for 5 to 10% of the total amount of cellulases produced by this organism. Together with EG I from Humicola insolens and T. reesei cellobiohydrolase I (CBH I), the enzyme is classified into family 7 of the glycosyl hydrolases, and it catalyses hydrolysis with a net retention of the anomeric configuration.The structure of the catalytic core domain (residues 1 to 371) of EG I from T. reesei has been determined at 3.6 A resolution by the molecular replacement method using the structures of T. reesei CBH I and H. insolens EG I as search models. By employing the 2-fold non-crystallographic symmetry (NCS), the structure was refined successfully, despite the limited resolution. The final model has an R-factor of 0.201 (Rfree 0.258).The structure of EG I reveals an extended, open substrate-binding cleft, rather than a tunnel as found in the homologous cellobiohydrolase CBH I. This confirms the earlier proposal that the tunnel-forming loops in CBH I have been deleted in EG I, which has resulted in an open active site in EG I, enabling it to function as an endoglucanase. Comparison of the structure of EG I with several related enzymes reveals structural similarities, and differences that relate to their biological function in degrading particular substrates. A possible structural explanation of the drastically different pH profiles of T. reesei and H. insolens EG I is proposed.
About this StructureAbout this Structure
1EG1 is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes., Kleywegt GJ, Zou JY, Divne C, Davies GJ, Sinning I, Stahlberg J, Reinikainen T, Srisodsuk M, Teeri TT, Jones TA, J Mol Biol. 1997 Sep 26;272(3):383-97. PMID:9325098
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