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PDBsum entry 1jqn

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Lyase PDB id
1jqn
Jmol
Contents
Protein chain
874 a.a. *
Ligands
ASP
DCO
Metals
_MN
Waters ×194
* Residue conservation analysis

References listed in PDB file
Key reference
Title Crystal structures of c4 form maize and quaternary complex of e. Coli phosphoenolpyruvate carboxylases.
Authors H.Matsumura, Y.Xie, S.Shirakata, T.Inoue, T.Yoshinaga, Y.Ueno, K.Izui, Y.Kai.
Ref. Structure, 2002, 10, 1721-1730. [DOI no: 10.1016/S0969-2126(02)00913-9]
PubMed id 12467579
Abstract
Phosphoenolpyruvate carboxylase (PEPC) catalyzes the first step in the fixation of atmospheric CO(2) during C(4) photosynthesis. The crystal structure of C(4) form maize PEPC (ZmPEPC), the first structure of the plant PEPCs, has been determined at 3.0 A resolution. The structure includes a sulfate ion at the plausible binding site of an allosteric activator, glucose 6-phosphate. The crystal structure of E. coli PEPC (EcPEPC) complexed with Mn(2+), phosphoenolpyruvate analog (3,3-dichloro-2-dihydroxyphosphinoylmethyl-2-propenoate), and an allosteric inhibitor, aspartate, has also been determined at 2.35 A resolution. Dynamic movements were found in the ZmPEPC structure, compared with the EcPEPC structure, around two loops near the active site. On the basis of these molecular structures, the mechanisms for the carboxylation reaction and for the allosteric regulation of PEPC are proposed.
Figure 1.
Figure 1. The Enzymatic Reaction and Structure of PEPC(A) The enzymatic reaction catalyzed by PEPC.(B) Proposed reaction mechanism catalyzed by PEPC.(C) PEP and its analog, DCDP.(D) The overall structure of ZmPEPC. Front view (left) of the tetrameric ZmPEPC generated by the crystallographic 2-fold axis. Side view (right) projected along the 2-fold axis.(E) Stereo view of the monomer structure of ZmPEPC projected in the same orientations as the brown subunit shown in (D). Sulfate is shown in CPK. Bundle A (a1, a4, a7, and a8), magenta; bundle B (a12, a13, a14, and a15), blue; the gated domain (a31, a32, a33, and a34), yellow; the flexible domain (residues 459-523), red; b barrel, green; other a helices, brown. The missing loops (124-140, 761-768, and 928-935) are shown as dots.
The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 1721-1730) copyright 2002.
Secondary reference #1
Title Plausible phosphoenolpyruvate binding site revealed by 2.6 a structure of mn2+-Bound phosphoenolpyruvate carboxylase from escherichia coli.
Authors H.Matsumura, M.Terada, S.Shirakata, T.Inoue, T.Yoshinaga, K.Izui, Y.Kai.
Ref. FEBS Lett, 1999, 458, 93-96.
PubMed id 10481043
Abstract
Secondary reference #2
Title Three-Dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition.
Authors Y.Kai, H.Matsumura, T.Inoue, K.Terada, Y.Nagara, T.Yoshinaga, A.Kihara, K.Tsumura, K.Izui.
Ref. Proc Natl Acad Sci U S A, 1999, 96, 823-828. [DOI no: 10.1073/pnas.96.3.823]
PubMed id 9927652
Full text Abstract
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.
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.
Secondary reference #3
Title Crystallization and preliminary X-Ray diffraction studies of c4-Form phosphoenolpyruvate carboxylase from maize.
Authors H.Matsumura, T.Nagata, M.Terada, S.Shirakata, T.Inoue, T.Yoshinaga, Y.Ueno, H.Saze, K.Izui, Y.Kai.
Ref. Acta Crystallogr D Biol Crystallogr, 1999, 55, 1937-1938. [DOI no: 10.1107/S0907444999010240]
PubMed id 10531501
Full text Abstract
Figure 1.
Figure 1 Crystals of C[4]-form PEPC obtained by the hanging-drop vapour-diffusion method.
The above figure is reproduced from the cited reference with permission from the IUCr
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