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1ayl
From Proteopedia
(New page: 200px<br /> <applet load="1ayl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ayl, resolution 1.8Å" /> '''PHOSPHOENOLPYRUVATE ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.49 4.1.1.49]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AYL OCA]]. | + | 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== | ||
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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: 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 Tue Oct 30 14:35:00 2007'' |
Revision as of 12:30, 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
Page seeded by OCA on Tue Oct 30 14:35:00 2007
