1ayl
From Proteopedia
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Revision as of 12:48, 30 October 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 ... [(full description)]
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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