1eg1
From Proteopedia
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'''ENDOGLUCANASE I FROM TRICHODERMA REESEI''' | '''ENDOGLUCANASE I FROM TRICHODERMA REESEI''' | ||
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[[Category: Kleywegt, G J.]] | [[Category: Kleywegt, G J.]] | ||
[[Category: Zou, J Y.]] | [[Category: Zou, J Y.]] | ||
| - | [[Category: | + | [[Category: Cellulose degradation]] |
| - | [[Category: | + | [[Category: Endoglucanase]] |
| - | [[Category: | + | [[Category: Mutation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:03:17 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:03, 2 May 2008
ENDOGLUCANASE I FROM TRICHODERMA REESEI
Overview
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 Structure
1EG1 is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 15:03:17 2008
