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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

Nature Structural Biology volume 3, pages 355–363 (1996)Cite this article

Abstract

We report the 1.8 Å crystal structure of adenosine triphosphate (ATP)–magnesium–oxalate bound phosphoenolpyruvate carboxykinase (PCK) from Escherichia coli. ATP binding induces a 20° 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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Authors and Affiliations

  1. Department of Biochemistry and, University of Saskatchewan, Saskatoon, 107 Wiggins Road, Saskatchewan, Canada, S7N5E5

    Leslie W. Tari, Allan Matte, Umarani Pugazhenthi & Louis T.J. Delbaere

  2. Department of Microbiology, University of Saskatchewan, Saskatoon, 107 Wiggins Road, Saskatchewan, Canada, S7N5E5

    Hughes Goldie

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  1. Leslie W. Tari
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Tari, L., Matte, A., Pugazhenthi, U. et al. Snapshot of an enzyme reaction intermediate in the structure of the ATP–Mg2+–oxalate ternary complex of Escherichia coli PEP carboxykinase. Nat Struct Mol Biol 3, 355–363 (1996). https://doi.org/10.1038/nsb0496-355

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