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PDBsum entry 1jqo

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protein ligands Protein-protein interface(s) links
Lyase PDB id
1jqo
Jmol
Contents
Protein chains
904 a.a. *
Ligands
SO4 ×2
* Residue conservation analysis
PDB id:
1jqo
Name: Lyase
Title: Crystal structure of c4-form phosphoenolpyruvate carboxylase maize
Structure: Phosphoenolpyruvate carboxylase. Chain: a, b. Synonym: phosphoenolpyruvate carboxylase 1, pepcase. Ec: 4.1.1.31
Source: Zea mays. Organism_taxid: 4577. Strain: b37. Tissue: leaves
Biol. unit: Dimer (from PDB file)
Resolution:
3.00Å     R-factor:   0.236     R-free:   0.272
Authors: H.Matsumura,Y.Kai
Key ref:
H.Matsumura et al. (2002). Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases. Structure, 10, 1721-1730. PubMed id: 12467579 DOI: 10.1016/S0969-2126(02)00913-9
Date:
07-Aug-01     Release date:   14-Jan-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04711  (CAPP1_MAIZE) -  Phosphoenolpyruvate carboxylase 1
Seq:
Struc:
 
Seq:
Struc:
970 a.a.
904 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.1.1.31  - Phosphoenolpyruvate carboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-
Phosphate
+ oxaloacetate
= H(2)O
+ phosphoenolpyruvate
+ HCO(3)(-)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     metabolic process   4 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
    reference    
 
 
DOI no: 10.1016/S0969-2126(02)00913-9 Structure 10:1721-1730 (2002)
PubMed id: 12467579  
 
 
Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases.
H.Matsumura, Y.Xie, S.Shirakata, T.Inoue, T.Yoshinaga, Y.Ueno, K.Izui, Y.Kai.
 
  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.
 
  Selected figure(s)  
 
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.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21491491 L.Dharmarajan, J.L.Kraszewski, B.Mukhopadhyay, and P.W.Dunten (2011).
Structure of an archaeal-type phosphoenolpyruvate carboxylase sensitive to inhibition by aspartate.
  Proteins, 79, 1820-1829.
PDB code: 3odm
19429552 D.S.Goltsman, V.J.Denef, S.W.Singer, N.C.VerBerkmoes, M.Lefsrud, R.S.Mueller, G.J.Dick, C.L.Sun, K.E.Wheeler, A.Zemla, B.J.Baker, L.Hauser, M.Land, M.B.Shah, M.P.Thelen, R.L.Hettich, and J.F.Banfield (2009).
Community genomic and proteomic analyses of chemoautotrophic iron-oxidizing "Leptospirillum rubarum" (Group II) and "Leptospirillum ferrodiazotrophum" (Group III) bacteria in acid mine drainage biofilms.
  Appl Environ Microbiol, 75, 4599-4615.  
  19923749 L.Dharmarajan, J.L.Kraszewski, B.Mukhopadhyay, and P.W.Dunten (2009).
Expression, purification and crystallization of an archaeal-type phosphoenolpyruvate carboxylase.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 1193-1196.  
18266899 B.Jacobs, S.Engelmann, P.Westhoff, and U.Gowik (2008).
Evolution of C(4) phosphoenolpyruvate carboxylase in Flaveria: determinants for high tolerance towards the inhibitor L-malate.
  Plant Cell Environ, 31, 793-803.  
16453061 J.Yuan, J.Sayegh, J.Mendez, L.Sward, N.Sanchez, S.Sanchez, G.Waldrop, and S.Grover (2006).
The regulatory role of residues 226-232 in phosphoenolpyruvate carboxylase from maize.
  Photosynth Res, 88, 73-81.  
16283377 R.Sánchez, A.Flores, and F.J.Cejudo (2006).
Arabidopsis phosphoenolpyruvate carboxylase genes encode immunologically unrelated polypeptides and are differentially expressed in response to drought and salt stress.
  Planta, 223, 901-909.  
16624802 W.Xu, S.Ahmed, H.Moriyama, and R.Chollet (2006).
The importance of the strictly conserved, C-terminal glycine residue in phosphoenolpyruvate carboxylase for overall catalysis: mutagenesis and truncation of GLY-961 in the sorghum C4 leaf isoform.
  J Biol Chem, 281, 17238-17245.  
15665330 A.Takahashi-Terada, M.Kotera, K.Ohshima, T.Furumoto, H.Matsumura, Y.Kai, and K.Izui (2005).
Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation.
  J Biol Chem, 280, 11798-11806.  
15725057 K.Izui, H.Matsumura, T.Furumoto, and Y.Kai (2004).
Phosphoenolpyruvate carboxylase: a new era of structural biology.
  Annu Rev Plant Biol, 55, 69-84.  
15516590 T.J.Ettema, K.S.Makarova, G.L.Jellema, H.J.Gierman, E.V.Koonin, M.A.Huynen, W.M.de Vos, and J.van der Oost (2004).
Identification and functional verification of archaeal-type phosphoenolpyruvate carboxylase, a missing link in archaeal central carbohydrate metabolism.
  J Bacteriol, 186, 7754-7762.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.