1OF4
Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate-binding module, TmCBM27
Summary for 1OF4
Entry DOI | 10.2210/pdb1of4/pdb |
Related | 1OF3 |
Descriptor | BETA-MANNOSIDASE, beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose, GLYCEROL, ... (5 entities in total) |
Functional Keywords | hydrolase/carbohydrate binding, mannan binding, carbohydrate binding module, polysaccharide degradation, hydrolase, hydrolase-carbohydrate binding complex |
Biological source | THERMOTOGA MARITIMA |
Total number of polymer chains | 1 |
Total formula weight | 21542.00 |
Authors | Boraston, A.B.,Revett, T.J.,Boraston, C.M.,Nurizzo, D.,Davies, G.J. (deposition date: 2003-04-07, release date: 2003-04-17, Last modification date: 2024-05-08) |
Primary citation | Boraston, A.B.,Revett, T.J.,Boraston, C.M.,Nurizzo, D.,Davies, G.J. Structural and Thermodynamic Dissection of Specific Mannan Recognition by a Carbohydrate Binding Module, Tmcbm27 Structure, 11:665-, 2003 Cited by PubMed Abstract: The 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. PubMed: 12791255DOI: 10.1016/S0969-2126(03)00100-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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