1of3

From Proteopedia

Revision as of 14:47, 5 November 2007

STRUCTURAL AND THERMODYNAMIC DISSECTION OF SPECIFIC MANNAN RECOGNITION BY A CARBOHYDRATE-BINDING MODULE, TMCBM27

Overview

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.

About this Structure

1OF3 is a Single protein structure of sequence from Thermotoga maritima with CA as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

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

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