1ayl
From Proteopedia
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|PDB= 1ayl |SIZE=350|CAPTION= <scene name='initialview01'>1ayl</scene>, resolution 1.8Å | |PDB= 1ayl |SIZE=350|CAPTION= <scene name='initialview01'>1ayl</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=ACT:Putative+Active+Site+Residues'>ACT</scene> | |SITE= <scene name='pdbsite=ACT:Putative+Active+Site+Residues'>ACT</scene> | ||
| - | |LIGAND= <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5 | + | |LIGAND= <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> |
|ACTIVITY= [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] | |ACTIVITY= [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] | ||
|GENE= | |GENE= | ||
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[[Category: protein-atp complex]] | [[Category: protein-atp complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:11:10 2008'' |
Revision as of 09:11, 23 March 2008
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| , resolution 1.8Å | |||||||
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| Sites: | |||||||
| Ligands: | , and | ||||||
| Activity: | Phosphoenolpyruvate carboxykinase (ATP), with EC number 4.1.1.49 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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