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The crystal structu...
The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 angstrom resolution, and a comparison with related enzymes
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- Kleywegt, GJ (författare)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi
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- Zou, JY (författare)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi
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- Divne, C (författare)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi
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Davies, GJ (författare)
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- Sinning, I (författare)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi
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Ståhlberg, J (författare)
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Reinikainen, T (författare)
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Srisodsuk, M (författare)
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- Teeri, TT (författare)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi
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- Jones, TA (författare)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi
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(creator_code:org_t)
- 1997
- 1997
- Engelska.
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Ingår i: JOURNAL OF MOLECULAR BIOLOGY. - 0022-2836. ; 272:3, s. 383-397
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Abstract
Ämnesord
Stäng
- 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.
Nyckelord
- cellulase; cellulose; endoglucanase; protein structure; X-ray crystallography; PROTEIN-STRUCTURE REFINEMENT; ACID-SEQUENCE SIMILARITIES; 3-DIMENSIONAL STRUCTURE; CELLOBIOHYDROLASE-I; ACTIVE-SITE; MACROMOLECULAR STRUCTURES; MOLECULAR REPLACEMENT; CELLULOLY
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Kleywegt, GJ
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Zou, JY
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Divne, C
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Davies, GJ
-
Sinning, I
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Ståhlberg, J
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visa fler...
-
Reinikainen, T
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Srisodsuk, M
-
Teeri, TT
-
Jones, TA
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visa färre...
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Uppsala universitet