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PDBsum entry 1qb4
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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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Plausible phosphoenolpyruvate binding site revealed by 2.6 a structure of mn2+-Bound phosphoenolpyruvate carboxylase from escherichia coli.
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Authors
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H.Matsumura,
M.Terada,
S.Shirakata,
T.Inoue,
T.Yoshinaga,
K.Izui,
Y.Kai.
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Ref.
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Febs Lett, 1999,
458,
93-96.
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PubMed id
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Abstract
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We have determined the crystal structure of Mn2+-bound Escherichia coli
phosphoenolpyruvate carboxylase (PEPC) using X-ray diffraction at 2.6 A
resolution, and specified the location of enzyme-bound Mn2+, which is essential
for catalytic activity. The electron density map reveals that Mn2+ is bound to
the side chain oxygens of Glu-506 and Asp-543, and located at the top of the
alpha/beta barrel in PEPC. The coordination sphere of Mn2+ observed in E. coli
PEPC is similar to that of Mn2+ found in the pyruvate kinase structure. The
model study of Mn2+-bound PEPC complexed with phosphoenolpyruvate (PEP) reveals
that the side chains of Arg-396, Arg-581 and Arg-713 could interact with PEP.
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Secondary reference #1
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Title
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Three-Dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition.
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Authors
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Y.Kai,
H.Matsumura,
T.Inoue,
K.Terada,
Y.Nagara,
T.Yoshinaga,
A.Kihara,
K.Tsumura,
K.Izui.
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Ref.
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Proc Natl Acad Sci U S A, 1999,
96,
823-828.
[DOI no: ]
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PubMed id
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Figure 6.
Fig. 6. Stereoview of the probable active site of PEPC.
H138, R396, K546, H579, R581, R587, R699, and aspartate are
shown in ball-and-stick representation. The figure is drawn in
the same orientation as Fig. 3a. The loop region of GRGGSIGRGG
is shown in blue. The missing loop from Lys-702 to Gly-708 is
shown as dots.
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Figure 7.
Fig. 7. (a) The C-terminal helix (  40), shown
in blue, is embedded in the PEPC monomer. The figure was
produced with MOLSCRIPT (37) and RASTER3D (38). (b) The
molecular surface, omitting the C-terminal helix coordinates,
was calculated with GRASP (25). The figure is shown in the same
orientation as a.
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