1ayl: Difference between revisions
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==Overview== | ==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 . | 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== | ==About this Structure== | ||
1AYL is a | 1AYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with OXL, MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxykinase_(ATP) Phosphoenolpyruvate carboxykinase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.49 4.1.1.49] Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AYL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: protein-atp complex]] | [[Category: protein-atp complex]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:35:11 2007'' | ||
