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PDBsum entry 1uwc
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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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Structure of a feruloyl esterase from aspergillus niger.
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Authors
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K.E.Mcauley,
A.Svendsen,
S.A.Patkar,
K.S.Wilson.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2004,
60,
878-887.
[DOI no: ]
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PubMed id
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Abstract
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The crystallographic structure of feruloyl esterase from Aspergillus niger has
been determined to a resolution of 1.5 A by molecular replacement. The protein
has an alpha/beta-hydrolase structure with a Ser-His-Asp catalytic triad; the
overall fold of the protein is very similar to that of the fungal lipases. The
structure of the enzyme-product complex was determined to a resolution of 1.08 A
and reveals dual conformations for the serine and histidine residues at the
active site.
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Figure 1.
Figure 1 Structure of arabinoxylan. The inset shows one type of
ferulic acid dimer that can be formed.
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Figure 2.
Figure 2 Diagrams of (a) open-form TlL, (b) FAE-III and (c)
closed-form TlL. The ribbon diagrams on the left are coloured
yellow for  -sheet,
red for  -helices
and violet for the lid helix. On the right are the
solvent-accessible surface representations. The surface is
coloured by residue type: blue, basic; red, acidic; yellow,
polar; grey, hydrophobic; green, catalytic triad. Figs. 2, 4,
5(b) and 6 were produced using PyMOL (DeLano, 2002[DeLano, W. L.
(2002). The PyMOL Molecular Graphics System.
http://www.pymol.org .]).
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2004,
60,
878-887)
copyright 2004.
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