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PDBsum entry 1of4
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Hydrolase/carbohydrate binding
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PDB id
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1of4
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate binding module, Tmcbm27.
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Authors
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A.B.Boraston,
T.J.Revett,
C.M.Boraston,
D.Nurizzo,
G.J.Davies.
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Ref.
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Structure, 2003,
11,
665-675.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 7.
Figure 7. A Schematic Showing the Interactions of TmCBM27
with G[2]M[5] (A) and Mannohexaose (B)Hydrogen bonds, dashed
lines; water molecules, filled circles. Binding subsites
referred to in the text are shown underneath the schematics with
brackets.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
665-675)
copyright 2003.
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