1qb4
From Proteopedia
|
CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE
Overview
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.
About this Structure
1QB4 is a Single protein structure of sequence from Escherichia coli with MN and ASP as ligands. Active as Phosphoenolpyruvate carboxylase, with EC number 4.1.1.31 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 00:32:57 2007
