1eg1

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[[Image:1eg1.gif|left|200px]]<br /><applet load="1eg1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1eg1.gif|left|200px]]
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caption="1eg1, resolution 3.6&Aring;" />
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'''ENDOGLUCANASE I FROM TRICHODERMA REESEI'''<br />
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{{Structure
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|PDB= 1eg1 |SIZE=350|CAPTION= <scene name='initialview01'>1eg1</scene>, resolution 3.6&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|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]
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|GENE=
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}}
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'''ENDOGLUCANASE I FROM TRICHODERMA REESEI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1EG1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EG1 OCA].
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1EG1 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=1EG1 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9325098 9325098]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9325098 9325098]
[[Category: Cellulase]]
[[Category: Cellulase]]
[[Category: Hypocrea jecorina]]
[[Category: Hypocrea jecorina]]
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[[Category: mutation]]
[[Category: mutation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:55:05 2008''

Revision as of 08:55, 20 March 2008


PDB ID 1eg1

Drag the structure with the mouse to rotate
, resolution 3.6Å
Ligands:
Activity: Cellulase, with EC number 3.2.1.4
Coordinates: save as pdb, mmCIF, xml



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

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