4eng
From Proteopedia
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STRUCTURE OF ENDOGLUCANASE V CELLOHEXAOSE COMPLEX
Overview
The structure of the catalytic core of the endoglucanase V (EGV) from, Humicola insolens has been determined by the method of multiple, isomorphous replacement at 1.5 A resolution. The final model, refined with, X-PLOR and PROLSQ, has a crystallographic R factor of 0.163 (R(free) =, 0.240) with deviations from stereochemical target values of 0.012 A and, 0.037 degrees for bonds and angles, respectively. The model was further, refined with SHELXL, including anisotropic modelling of the protein-atom, temperature factors, to give a final model with an R factor of 0.105 and, an R(free) of 0.154. The initial isomorphous replacement electron-density, map was poor and uninterpretable but was improved by the use of, synchrotron data collected at a wavelength chosen so as to optimize the f", contribution of the anomalous scattering from the heavy atoms. The, structure of H. insolens EGV consists of a six-stranded beta-barrel, domain, similar to that found in a family of plant defence proteins, linked by a number of disulfide-bonded loop regions. A long open groove, runs across the surface of the enzyme either side of which lie the, catalytic aspartate residues. The 9 A separation of the catalytic, carboxylate groups is consistent with the observation that EGV catalyzes, the hydrolysis of the cellulose, beta(1-->4) links with inversion of, configuration at the anomeric C1 atom. This structure is the first, representative from the glycosyl hydrolase family 45.
About this Structure
4ENG is a Single protein structure of sequence from Humicola insolens with CTR as ligand. Active as Cellulase, with EC number 3.2.1.4 Full crystallographic information is available from OCA.
Reference
Structure determination and refinement of the Humicola insolens endoglucanase V at 1.5 A resolution., Davies GJ, Dodson G, Moore MH, Tolley SP, Dauter Z, Wilson KS, Rasmussen G, Schulein M, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):7-17. PMID:15299721
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