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PDBsum entry 2fwm
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Oxidoreductase
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PDB id
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2fwm
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References listed in PDB file
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Key reference
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Title
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Determination of the crystal structure of enta, A 2,3-Dihydro-2,3-Dihydroxybenzoic acid dehydrogenase from escherichia coli.
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Authors
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J.A.Sundlov,
J.A.Garringer,
J.M.Carney,
A.S.Reger,
E.J.Drake,
W.L.Duax,
A.M.Gulick.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2006,
62,
734-740.
[DOI no: ]
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PubMed id
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Abstract
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The Escherichia coli enterobactin synthetic cluster is composed of six proteins,
EntA-EntF, that form the enterobactin molecule from three serine molecules and
three molecules of 2,3-dihydroxybenzoic acid (DHB). EntC, EntB and EntA catalyze
the three-step synthesis of DHB from chorismate. EntA is a member of the
short-chain oxidoreductase (SCOR) family of proteins and catalyzes the final
step in DHB synthesis, the NAD+-dependent oxidation of
2,3-dihydro-2,3-dihydroxybenzoic acid to DHB. The structure of EntA has been
determined by multi-wavelength anomalous dispersion methods. Here, the 2.0 A
crystal structure of EntA in the unliganded form is presented. Analysis of the
structure in light of recent structural and bioinformatic analysis of other
members of the SCOR family provides insight into the residues involved in
cofactor and substrate binding.
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Figure 3.
Figure 3 Structure of the EntA monomer and tetramer. (a) Ribbon
diagram of the EntA monomer. The central  -sheet
is shown in red, while the surrounding helices are shown in
blue. The secondary-structural elements are labeled. Note that
helices  1
and 3
are not present in the EntA structure; in accordance with
secondary-structure nomenclature for prior SCOR proteins (Duax
et al., 2000[Duax, W. L., Ghosh, D. & Pletnev, V. (2000). Vitam.
Horm. 58, 121-148.]), the helices are labeled 2,
4,
5,
6,
and 7.
(b) The EntA tetramer is shown viewed down one twofold axis of
222 crystallographic symmetry. The two top and two bottom
subunits interact around the four-helix bundle formed by helices
5
and 6.
The C-terminal loops and 7
form interactions between dimers.
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Figure 4.
Figure 4 Proposed substrate-binding pocket of EntA. The
residues of the EntA protein predicted by covariance analysis to
contribute to 2,3-DHDHB-specific binding are labeled. The
cofactor molecule (shown in orange) was modeled into the
unliganded EntA structure by superimposing the 7 -hydroxysteroid
dehydrogenase (PDB code 1fmc ) structure onto the EntA molecule.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
734-740)
copyright 2006.
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