5CEL
CBH1 (E212Q) CELLOTETRAOSE COMPLEX
Summary for 5CEL
| Entry DOI | 10.2210/pdb5cel/pdb |
| Related | 1CEL 6CEL 7CEL |
| Related PRD ID | PRD_900011 |
| Descriptor | 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE I, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | hydrolase, cellulose degradation, glycosidase, glycoprotein, glycosylated protein |
| Biological source | Hypocrea jecorina |
| Total number of polymer chains | 1 |
| Total formula weight | 47739.98 |
| Authors | Divne, C.,Stahlberg, J.,Jones, T.A. (deposition date: 1997-09-24, release date: 1997-12-24, Last modification date: 2024-10-30) |
| Primary citation | Divne, C.,Stahlberg, J.,Teeri, T.T.,Jones, T.A. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei. J.Mol.Biol., 275:309-325, 1998 Cited by PubMed Abstract: 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 the fungus Trichoderma reesei. Three high-resolution crystal structures of different catalytically deficient mutants of CBHI in complex with cellotetraose, cellopentaose and cellohexaose have been refined at 1.9, 1.7 and 1.9 A resolution, respectively. The observed binding of cellooligomers in the tunnel allowed unambiguous identification of ten well-defined subsites for glucosyl units that span a length of approximately 50 A. All bound oligomers have the same directionality and orientation, and the positions of the glucosyl units in each binding site agree remarkably well between the different complexes. The binding mode observed here corresponds to that expected during productive binding of a cellulose chain. The structures support the hypothesis that hydrolysis by CBHI proceeds from the reducing towards the non-reducing end of a cellulose chain, and they provide a structural explanation for the observed distribution of initial hydrolysis products. PubMed: 9466911DOI: 10.1006/jmbi.1997.1437 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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