1CEL

THE THREE-DIMENSIONAL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI

Summary for 1CEL

• Entry DOI: 10.2210/pdb1cel/pdb
• Descriptor: 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE I, 2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: hydrolase(o-glycosyl)
• Biological source: Trichoderma reesei (Hypocrea jecorina)
• Total number of polymer chains: 2
• Total formula weight: 93364.41

Authors

Divne, C.,Jones, T.A. (deposition date: 1994-05-17, release date: 1994-11-01, Last modification date: 2024-10-30)

Primary citation

Divne, C.,Stahlberg, J.,Reinikainen, T.,Ruohonen, L.,Pettersson, G.,Knowles, J.K.,Teeri, T.T.,Jones, T.A.
The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei.
Science, 265:524-528, 1994

PubMed Abstract: 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.

PubMed: 8036495

Experimental method

X-RAY DIFFRACTION (1.8 Å)