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1OF4

Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate-binding module, TmCBM27

Summary for 1OF4
Entry DOI10.2210/pdb1of4/pdb
Related1OF3
DescriptorBETA-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 Keywordshydrolase/carbohydrate binding, mannan binding, carbohydrate binding module, polysaccharide degradation, hydrolase, hydrolase-carbohydrate binding complex
Biological sourceTHERMOTOGA MARITIMA
Total number of polymer chains1
Total formula weight21542.00
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 citationBoraston, 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: 12791255
DOI: 10.1016/S0969-2126(03)00100-X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

226707

數據於2024-10-30公開中

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