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Structural and Thermodynamic Dissection of Specific Mannan Recognition by a Carbohydrate Binding Module,TmCBM27

Authors
Journal
Structure
0969-2126
Publisher
Elsevier
Publication Date
Volume
11
Issue
6
Identifiers
DOI: 10.1016/s0969-2126(03)00100-x

Abstract

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 as 10 5–10 6 M −1) to β-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-α-D-galactosyl-mannopentaose complex at 2.0 Å, 1.6 Å, and 1.35 Å, 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.

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