Crystal structures of Clostridium thermocellum xyloglucanase, XGH74A, reveal the structural basis for xyloglucan recognition and degradation
2006 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 281, no 34, 24922-24933 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2006. Vol. 281, no 34, 24922-24933 p.
END-SPECIFIC CELLOBIOHYDROLASE; PLANT-CELL WALL; GLYCOSYL HYDROLASES; CELLULOSE SURFACES; EXPRESSION; CLONING; CLASSIFICATION; ENDOGLUCANASE; BIOSYNTHESIS; PURIFICATION
IdentifiersURN: urn:nbn:se:kth:diva-6910DOI: 10.1074/jbc.M603583200ISI: 000239847800085ScopusID: 2-s2.0-33747635388OAI: oai:DiVA.org:kth-6910DiVA: diva2:11756
QC 201006242007-03-222007-03-222010-12-06Bibliographically approved