1eg1: Difference between revisions
New page: left|200px<br /><applet load="1eg1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eg1, resolution 3.6Å" /> '''ENDOGLUCANASE I FROM ... |
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[[Image:1eg1.gif|left|200px]]<br /><applet load="1eg1" size=" | [[Image:1eg1.gif|left|200px]]<br /><applet load="1eg1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1eg1, resolution 3.6Å" /> | caption="1eg1, resolution 3.6Å" /> | ||
'''ENDOGLUCANASE I FROM TRICHODERMA REESEI'''<br /> | '''ENDOGLUCANASE I FROM TRICHODERMA REESEI'''<br /> | ||
==Overview== | ==Overview== | ||
Cellulose is the most abundant polymer in the biosphere. Although | 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== | ==About this Structure== | ||
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 NAG 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:// | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: Hypocrea jecorina]] | [[Category: Hypocrea jecorina]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jones, T | [[Category: Jones, T A.]] | ||
[[Category: Kleywegt, G | [[Category: Kleywegt, G J.]] | ||
[[Category: Zou, J | [[Category: Zou, J Y.]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: cellulose degradation]] | [[Category: cellulose degradation]] | ||
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[[Category: mutation]] | [[Category: mutation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:21 2008'' |