1ayl
From Proteopedia
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Revision as of 13:47, 5 November 2007
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PHOSPHOENOLPYRUVATE CARBOXYKINASE
Overview
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.
About this Structure
1AYL is a Single protein structure of sequence from Escherichia coli with OXL, MG and ATP as ligands. Active as Phosphoenolpyruvate carboxykinase (ATP), with EC number 4.1.1.49 Structure known Active Site: ACT. Full crystallographic information is available from OCA.
Reference
Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase., Tari LW, Matte A, Pugazhenthi U, Goldie H, Delbaere LT, Nat Struct Biol. 1996 Apr;3(4):355-63. PMID:8599762
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