ISDA: 1QB4

Deposition Date 1999-04-30

Release Date 2002-05-01

Last Version Date 2024-02-14

Entry Detail

PDB ID:

1QB4

Keywords:

LYASE

Title:

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

Biological Source:

Source Organism(s):

Escherichia coli (Taxon ID: 562)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.60 Å

R-Value Free:

0.26

R-Value Work:

0.22

R-Value Observed:

0.22

Space Group:

I 2 2 2

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:PHOSPHOENOLPYRUVATE CARBOXYLA
Gene (Uniprot):ppc
Chain IDs:A
Chain Length:883
Number of Molecules:1
Biological Source:Escherichia coli

UniProt ID:P00864 Pfam ID:PF00311 EC:4.1.1.31

Ligand Molecules

ASP

Primary Citation

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.Show

FEBS Lett. 458 93 96 (1999)

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

Abstact

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.

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Protein

Chemical

Disease

Primary Citation of related structures

Abstact

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