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High-resolution crystal structures reveal how a cellulose chain is bound in the 50 angstrom long tunnel of cellobiohydrolase I from Trichoderma reesei
Uppsala University.
Uppsala University.
Uppsala University.
Uppsala University.
1998 (English)In: JOURNAL OF MOLECULAR BIOLOGY, ISSN 0022-2836, Vol. 275, no 2, 309-325 p.Article in journal (Other scientific) Published
Abstract [en]

Detailed information has been obtained, by means of protein X-ray crystallography, on how a cellulose chain is bound in the cellulose-binding tunnel of cellobiohydrolase I (CBHI), the major cellulase in the hydrolysis of native, crystalline cellulose by t

Place, publisher, year, edition, pages
ACADEMIC PRESS LTD , 1998. Vol. 275, no 2, 309-325 p.
Keyword [en]
cellulase; cellobiohydrolase; oligosaccharide complex; active-site mutant; crystal structure; ACID-SEQUENCE SIMILARITIES; ELECTRON-DENSITY MAPS; FREE R-VALUE; BINDING DOMAIN; 3-DIMENSIONAL STRUCTURE; QM-9414; MODEL; IDENTIFICATION; CLASSIFICATION; REFINEM
Identifiers
URN: urn:nbn:se:uu:diva-79414OAI: oai:DiVA.org:uu-79414DiVA: diva2:107327
Note
Addresses: Jones TA, Uppsala Univ, Ctr Biomed, Dept Biol Mol, POB 590, S-75124 Uppsala, Sweden. Uppsala Univ, Ctr Biomed, Dept Biol Mol, S-75124 Uppsala, Sweden. VTT Biotechnol & Food Res, FIN-02044 Espoo, Finland.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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