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Publication Abstract from PubMed

The enzymatic degradation of plant cell walls plays a central role in the carbon cycle and is of increasing environmental and industrial significance. The enzymes that catalyse this process include xylanases which degrade xylan, a beta-1,4-D-xylose polymer that is decorated with various sugars. Although xylanases efficiently hydrolyse unsubstituted xylans, these enzymes are unable to access highly decorated forms of the polysaccharide, such as arabinoxylans that contain arabinofuranose decorations. Here we show that a Clostridium thermocellum enzyme, designated CtXyl5A, hydrolyses arabinoxylans but does not attack unsubstituted xylans. Analysis of the reaction products generated by CtXyl5A showed that all the oligosaccharides contain an O3 arabinose linked to the reducing end xylose. The crystal structure of the catalytic module (CtGH5) of CtXyl5A, appended to a family 6 non-catalytic carbohydrate binding module (CtCBM6), showed that CtGH5 displays a canonical (beta/alpha)8-barrel fold with the substrate binding cleft running along the surface of the protein. The catalytic apparatus is housed in the centre of the cleft. Adjacent to the -1 subsite is a pocket that could accommodate an L-arabinofuranose linked alpha-1,3 to the active site xylose, which is likely to function as a key specificity determinant. CtCBM6, which adopts a beta-nsandwich fold, recognizes the termini of xylo- and gluco-configured oligosaccharides, consistent with the pocket topology displayed by the ligand binding site. In contrast to typical modular glycoside hydrolases, there is an extensive hydrophobic interface between CtGH5 and CtCBM6, and thus the two modules cannot function as independent entities.

The structure and function of an arabinoxylan-specific xylanase.,Correia MA, Mazumder K, Bras JL, Firbank SJ, Zhu Y, Lewis RJ, York WS, Fontes CM, Gilbert HJ J Biol Chem. 2011 Mar 4. PMID:21378160^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.