1AYL

PHOSPHOENOLPYRUVATE CARBOXYKINASE

Summary for 1AYL

• Entry DOI: 10.2210/pdb1ayl/pdb
• Descriptor: PHOSPHOENOLPYRUVATE CARBOXYKINASE, OXALATE ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: p-loop, protein-atp complex, nucleotide-triphosphate hydrolase, kinase (transphosphorylating)
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P22259
• Total number of polymer chains: 1
• Total formula weight: 60415.76

Authors

Tari, L.W.,Pugazenthi, U.,Goldie, H.,Delbaere, L.T.J. (deposition date: 1995-12-07, release date: 1997-01-11, Last modification date: 2024-02-07)

Primary citation

Tari, L.W.,Matte, A.,Pugazhenthi, U.,Goldie, H.,Delbaere, L.T.
Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase.
Nat.Struct.Biol., 3:355-363, 1996

PubMed Abstract: We report the 1.8 A crystal structure of adenosine triphosphate (ATP)-magnesium-oxalate bound phosphoenolpyruvate carboxykinase (PCK) from Escherichia coli. ATP binding induces a 20 degree hinge-like rotation of the N- and C-terminal domains which closes the active-site cleft. PCK possesses a novel nucleotide-binding fold, particularly in the adenine-binding region, where the formation of a cis backbone torsion angle in a loop glycine residue promotes intimate contacts between the adenine-binding loop and adenine, while stabilizing a syn conformation of the base. This complex represents a reaction intermediate analogue along the pathway of the conversion of oxaloacetate to phosphoenolpyruvate, and provides insight into the mechanistic details of the chemical reaction catalysed by this enzyme.

PubMed: 8599762
DOI: 10.1038/nsb0496-355

Experimental method

X-RAY DIFFRACTION (1.8 Å)