| | |  | | | | Record from Web of Science® | | | | | | |
| Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg2+-oxalate ternary complex of Escherichia coli PEP carboxykinase |
|
|
| Author(s): Tari LW, Matte A, Pugazhenthi U, Goldie H, Delbaere LTJ |
| Source: NATURE STRUCTURAL BIOLOGY Volume: 3 Issue: 4 Pages: 355-363 Published: APR 1996 |
| Times Cited: 56 References: 55 |
| Abstract: We report the 1.8 Angstrom crystal structure of adenosine triphosphate (ATP)-magnesium-oxalate bound phosphoenolpyruvate carboxykinase (PCK) from Escherichia coli. ATP binding induces a 20 degrees 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. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV SASKATCHEWAN, DEPT BIOCHEM, SASKATOON, SK S7N 5E5 CANADA
2. UNIV SASKATCHEWAN, DEPT MICROBIOL, SASKATOON, SK S7N 5E5 CANADA |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: UD310 |
| ISSN: 1072-8368 |
|
| | | | | | | | | Record from Web of Science® | | | | | | | | | |