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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'''ENDOGLUCANASE I FROM TRICHODERMA REESEI'''<br />
'''ENDOGLUCANASE I FROM TRICHODERMA REESEI'''<br />


==Overview==
==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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EG1 OCA].  
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.A.]]
[[Category: Jones, T A.]]
[[Category: Kleywegt, G.J.]]
[[Category: Kleywegt, G J.]]
[[Category: Zou, J.Y.]]
[[Category: Zou, J Y.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: cellulose degradation]]
[[Category: cellulose degradation]]
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[[Category: mutation]]
[[Category: mutation]]


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