1ayl
From Proteopedia
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[[Image:1ayl.gif|left|200px]] | [[Image:1ayl.gif|left|200px]] | ||
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'''PHOSPHOENOLPYRUVATE CARBOXYKINASE''' | '''PHOSPHOENOLPYRUVATE CARBOXYKINASE''' | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8599762 8599762] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8599762 8599762] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Phosphoenolpyruvate carboxykinase (ATP)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Delbaere, L T.J.]] | [[Category: Delbaere, L T.J.]] | ||
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[[Category: Pugazenthi, U.]] | [[Category: Pugazenthi, U.]] | ||
[[Category: Tari, L W.]] | [[Category: Tari, L W.]] | ||
| - | [[Category: | + | [[Category: Nucleotide-triphosphate hydrolase]] |
| - | + | [[Category: P-loop]] | |
| - | [[Category: | + | [[Category: Protein-atp complex]] |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:51:06 2008'' |
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Revision as of 07:51, 2 May 2008
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 Page seeded by OCA on Fri May 2 10:51:06 2008
