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1qb4

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1qb4, resolution 2.60Å ()
Ligands: ,
Gene: K12 (Escherichia coli)
Activity: Phosphoenolpyruvate carboxylase, with EC number 4.1.1.31
Related: 1fiy
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE

Publication Abstract from PubMed

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.

Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coli., Matsumura H, Terada M, Shirakata S, Inoue T, Yoshinaga T, Izui K, Kai Y, FEBS Lett. 1999 Sep 17;458(2):93-6. PMID:10481043

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1qb4 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Matsumura H, Terada M, Shirakata S, Inoue T, Yoshinaga T, Izui K, Kai Y. Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coli. FEBS Lett. 1999 Sep 17;458(2):93-6. PMID:10481043

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