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- Kleywegt, GJUppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi (author)
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
- Article/chapterEnglish1997
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- 1997
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- LIBRIS-ID:oai:DiVA.org:uu-84930
- https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-84930URI
- https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-84924URI
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- Language:English
- Summary in:English
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- 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.
Subject headings and genre
- 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
Added entries (persons, corporate bodies, meetings, titles ...)
- Zou, JYUppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi (author)
- Divne, CUppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi (author)
- Davies, GJ (author)
- Sinning, IUppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi (author)
- Ståhlberg, J (author)
- Reinikainen, T (author)
- Srisodsuk, M (author)
- Teeri, TTUppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi (author)
- Jones, TAUppsala universitet,Institutionen för cell- och molekylärbiologi,Strukturell molekylärbiologi (author)
- Uppsala universitetInstitutionen för cell- och molekylärbiologi (creator_code:org_t)
Related titles
- In:JOURNAL OF MOLECULAR BIOLOGY272:3, s. 383-3970022-2836
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