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PDBsum entry 1v35
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Oxidoreductase
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PDB id
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1v35
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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 basis for the variation in triclosan affinity to enoyl reductases.
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Authors
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L.S.Pidugu,
M.Kapoor,
N.Surolia,
A.Surolia,
K.Suguna.
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Ref.
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J Mol Biol, 2004,
343,
147-155.
[DOI no: ]
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PubMed id
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Abstract
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Bacteria synthesize fatty acids in a dissociated type pathway different from
that in humans. Enoyl acyl carrier protein reductase, which catalyzes the final
step of fatty acid elongation, has been validated as a potential anti-microbial
drug target. Triclosan is known to inhibit this enzyme effectively. Precise
characterization of the mode of triclosan binding is required to develop highly
specific inhibitors. With this in view, interactions between triclosan, the
cofactor NADH/NAD+ and the enzyme from five different species, one plant and
four of microbial origin, have been examined in the available crystal
structures. A comparison of these structures shows major structural differences
at the substrate/inhibitor/cofactor-binding loop. The analysis reveals that the
conformation of this flexible loop and the binding affinities of triclosan to
each of these enzymes are strongly correlated.
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Figure 9.
Figure 9. Hydrogen bonds between the adenine ring of NAD
C
and the protein in pfENR.
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Figure 10.
Figure 10. 2FoKFc electron den-
sity map contoured at 1.5s for
cofactor NAD
C
and inhibitor tri-
closan. The Figures have been
generated using the program BOB-
SCRIPT
41
and rendered using
RASTER3D.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2004,
343,
147-155)
copyright 2004.
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Secondary reference #1
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Title
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Kinetic and structural analysis of the increased affinity of enoyl-Acp (acyl-Carrier protein) reductase for triclosan in the presence of NAD+.
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Authors
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M.Kapoor,
P.L.Mukhi,
N.Surolia,
K.Suguna,
A.Surolia.
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Ref.
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Biochem J, 2004,
381,
725-733.
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PubMed id
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