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Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate-binding module, TmCBM27Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate-binding module, TmCBM27
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe C-terminal 176 amino acids of a Thermotoga maritima mannanase (Man5) constitute a carbohydrate binding module (CBM) that has been classified into CBM family 27. The isolated CBM27 domain, named TmCBM27, binds tightly (K(a)s 10(5)-10(6) M(-1)) to beta-1, 4-mannooligosaccharides, carob galactomannan, and konjac glucomannan, but not to cellulose (insoluble and soluble) or soluble birchwood xylan. The X-ray crystal structures of native TmCBM27, a TmCBM27-mannohexaose complex, and a TmCBM27-6(3),6(4)-alpha-D-galactosyl-mannopentaose complex at 2.0 A, 1.6 A, and 1.35 A, respectively, reveal the basis of TmCBM27's specificity for mannans. In particular, the latter complex, which is the first structure of a CBM in complex with a branched plant cell wall polysaccharide, illustrates how the architecture of the binding site can influence the recognition of naturally substituted polysaccharides. Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate binding module, TmCBM27.,Boraston AB, Revett TJ, Boraston CM, Nurizzo D, Davies GJ Structure. 2003 Jun;11(6):665-75. PMID:12791255[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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