1ayl

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{{STRUCTURE_1ayl| PDB=1ayl | SCENE= }}
{{STRUCTURE_1ayl| PDB=1ayl | SCENE= }}
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'''PHOSPHOENOLPYRUVATE CARBOXYKINASE'''
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===PHOSPHOENOLPYRUVATE CARBOXYKINASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8599762 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8599762}}
==About this Structure==
==About this Structure==
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[[Category: P-loop]]
[[Category: P-loop]]
[[Category: Protein-atp complex]]
[[Category: Protein-atp complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:51:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:52:12 2008''

Revision as of 14:52, 30 June 2008

Image:1ayl.png

Template:STRUCTURE 1ayl

PHOSPHOENOLPYRUVATE CARBOXYKINASE

Template:ABSTRACT PUBMED 8599762

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 Mon Jun 30 17:52:12 2008

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