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Sökning: WFRF:(Montanier Cedric) > A novel, noncatalyt...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003601naa a2200433 4500
001oai:DiVA.org:kth-179860
003SwePub
008160104s2011 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-1798602 URI
0247 a https://doi.org/10.1074/jbc.M110.2173722 DOI
040 a (SwePub)kth
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Montanier, Cedric Y.4 aut
2451 0a A novel, noncatalytic carbohydrate-binding module displays specificity for galactose-containing polysaccharides through calcium-mediated oligomerization
264 1b American Society for Biochemistry and Molecular Biology,c 2011
338 a print2 rdacarrier
500 a QC 20160126
520 a The enzymic degradation of plant cell walls plays a central role in the carbon cycle and is of increasing environmental and industrial significance. The catalytic modules of enzymes that catalyze this process are generally appended to noncatalytic carbohydrate-binding modules (CBMs). CBMs potentiate the rate of catalysis by bringing their cognate enzymes into intimate contact with the target substrate. A powerful plant cell wall-degrading system is the Clostridium thermocellum multienzyme complex, termed the "cellulosome." Here, we identify a novel CBM (CtCBM62) within the large C. thermocellum cellulosomal protein Cthe_2193 (defined as CtXyl5A), which establishes a new CBM family. Phylogenetic analysis of CBM62 members indicates that a circular permutation occurred within the family. CtCBM62 binds to D-galactose and L-arabinopyranose in either anomeric configuration. The crystal structures of CtCBM62, in complex with oligosaccharides containing alpha- and beta-galactose residues, show that the ligand-binding site in the beta-sandwich protein is located in the loops that connect the two beta-sheets. Specificity is conferred through numerous interactions with the axial O4 of the target sugars, a feature that distinguishes galactose and arabinose from the other major sugars located in plant cell walls. CtCBM62 displays tighter affinity for multivalent ligands compared with molecules containing single galactose residues, which is associated with precipitation of these complex carbohydrates. These avidity effects, which confer the targeting of polysaccharides, are mediated by calcium-dependent oligomerization of the CBM.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
7001 a Correia, Marcia A. S.4 aut
7001 a Flint, James E.4 aut
7001 a Zhu, Yanping4 aut
7001 a Basle, Arnaud4 aut
7001 a McKee, Lauren,d 1985-u Newcastle University, United Kingdom; University of Georgia, United States4 aut0 (Swepub:kth)u1nbm728
7001 a Prates, Jose A. M.4 aut
7001 a Polizzi, Samuel J.4 aut
7001 a Coutinho, Pedro M.4 aut
7001 a Lewis, Richard J.4 aut
7001 a Henrissat, Bernard4 aut
7001 a Fontes, Carlos M. G. A.4 aut
7001 a Gilbert, Harry J.4 aut
7102 a Newcastle University, United Kingdom; University of Georgia, United States4 org
7730 t Journal of Biological Chemistryd : American Society for Biochemistry and Molecular Biologyg 286:25q 286:25x 0021-9258x 1083-351X
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-179860
8564 8u https://doi.org/10.1074/jbc.M110.217372

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