1cel
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(New page: 200px<br /><applet load="1cel" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cel, resolution 1.8Å" /> '''THE THREE-DIMENSIONAL...)
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Revision as of 10:16, 20 November 2007
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THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI
Overview
Cellulose is the major polysaccharide of plants where it plays a, predominantly structural role. A variety of highly specialized, microorganisms have evolved to produce enzymes that either synergistically, or in complexes can carry out the complete hydrolysis of cellulose. The, structure of the major cellobiohydrolase, CBHI, of the potent cellulolytic, fungus Trichoderma reesei has been determined and refined to 1.8 angstrom, resolution. The molecule contains a 40 angstrom long active site tunnel, that may account for many of the previously poorly understood macroscopic, properties of the enzyme and its interaction with solid cellulose. The, active site residues were identified by solving the structure of the, enzyme complexed with an oligosaccharide, o-iodobenzyl-1-thio-beta-cellobioside. The three-dimensional structure is, very similar to a family of bacterial beta-glucanases with the main-chain, topology of the plant legume lectins.
About this Structure
1CEL is a Single protein structure of sequence from [1] with NAG, GLC, CA and IBZ as ligands. Active as Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 Full crystallographic information is available from OCA.
Reference
The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei., Divne C, Stahlberg J, Reinikainen T, Ruohonen L, Pettersson G, Knowles JK, Teeri TT, Jones TA, Science. 1994 Jul 22;265(5171):524-8. PMID:8036495
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