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2CN3

Crystal Structures of Clostridium thermocellum Xyloglucanase

Summary for 2CN3
Entry DOI10.2210/pdb2cn3/pdb
Related2CN2
DescriptorBETA-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 Keywordsglycosylhydrolase, hydrolase, family gh74, xyloglucanase
Biological sourceCLOSTRIDIUM THERMOCELLUM
Total number of polymer chains2
Total formula weight167065.72
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 citationMartinez-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: 16772298
DOI: 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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