1QB4

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

Summary for 1QB4

• Entry DOI: 10.2210/pdb1qb4/pdb
• Related: 1FIY
• Descriptor: PHOSPHOENOLPYRUVATE CARBOXYLASE, MANGANESE (II) ION, ASPARTIC ACID, ... (4 entities in total)
• Functional Keywords: alpha beta barrel, lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 99363.53

Authors

Matsumura, H.,Terada, M.,Shirakata, S.,Inoue, T.,Yoshinaga, T.,Izui, K.,Kai, Y. (deposition date: 1999-04-30, release date: 2002-05-01, Last modification date: 2024-02-14)

Primary citation

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., 458:93-96, 1999

PubMed Abstract: 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.

PubMed: 10481043
DOI: 10.1016/S0014-5793(99)01103-5

Experimental method

X-RAY DIFFRACTION (2.6 Å)