2CN3
Crystal Structures of Clostridium thermocellum Xyloglucanase
Summary for 2CN3
Entry DOI | 10.2210/pdb2cn3/pdb |
Related | 2CN2 |
Descriptor | BETA-1,4-XYLOGLUCAN HYDROLASE, alpha-D-xylopyranose-(1-6)-beta-D-glucopyranose-(1-4)-[alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-[beta-D-galactopyranose-(1-2)-alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-xylopyranose-(1-6)-beta-D-glucopyranose-(1-4)-[beta-D-galactopyranose-(1-2)-alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-[beta-D-galactopyranose-(1-2)-alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | glycosylhydrolase, hydrolase, family gh74, xyloglucanase |
Biological source | CLOSTRIDIUM THERMOCELLUM |
Total number of polymer chains | 2 |
Total formula weight | 167065.72 |
Authors | Martinez-Fleites, C.,Taylor, E.J.,Guerreiro, C.I.P.D.,Prates, J.A.M.,Ferreira, L.M.A.,Fontes, C.M.G.A.,Baumann, M.J.,Brumer, H.,Davies, G.J. (deposition date: 2006-05-17, release date: 2006-05-22, Last modification date: 2023-12-13) |
Primary citation | Martinez-Fleites, C.,Taylor, E.J.,Guerreiro, C.I.P.D.,Prates, J.A.M.,Ferreira, L.M.A.,Fontes, C.M.G.A.,Baumann, M.J.,Brumer, H.,Davies, G.J. Crystal Structures of Clostridium Thermocellum Xyloglucanase, Xgh74A, Reveal the Structural Basis for Xyloglucan Recognition and Degradation J.Biol.Chem., 281:24922-, 2006 Cited by PubMed Abstract: The enzymatic degradation of the plant cell wall is central both to the natural carbon cycle and, increasingly, to environmentally friendly routes to biomass conversion, including the production of biofuels. The plant cell wall is a complex composite of cellulose microfibrils embedded in diverse polysaccharides collectively termed hemicelluloses. Xyloglucan is one such polysaccharide whose hydrolysis is catalyzed by diverse xyloglucanases. Here we present the structure of the Clostridium thermocellum xyloglucanase Xgh74A in both apo and ligand-complexed forms. The structures, in combination with mutagenesis data on the catalytic residues and the kinetics and specificity of xyloglucan hydrolysis reveal a complex subsite specificity accommodating seventeen monosaccharide moieties of the multibranched substrate in an open substrate binding terrain. PubMed: 16772298DOI: 10.1074/JBC.M603583200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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