Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.
- 1 November 1989
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 86 (22) , 8635-8639
- https://doi.org/10.1073/pnas.86.22.8635
Abstract
The structure of isocitrate dehydrogenase [threo-DS-isocitrate: NADP+ oxidoreductase (decarboxylating), EC 1.1.1.42] from Escherichia coli has been solved and refined at 2.5 A resolution and is topologically different from that of any other dehydrogenase. This enzyme, a dimer of identical 416-residue subunits, is inactivated by phosphorylation at Ser-113, which lies at the edge of an interdomain pocket that also contains many residues conserved between isocitrate dehydrogenase and isopropylmalate dehydrogenase. Isocitrate dehydrogenase contains an unusual clasp-like domain in which both polypeptide chains in the dimer interlock. Based on the structure of isocitrate dehydrogenase and conservation with isopropylmalate dehydrogenase, we suggest that the active site lies in an interdomain pocket close to the phosphorylation site.This publication has 41 references indexed in Scilit:
- Structural changes in glycogen phosphorylase induced by phosphorylationNature, 1988
- Structure of the human class I histocompatibility antigen, HLA-A2Nature, 1987
- Molecular Cloning and Nucleotide Sequence of the 3-Isopropylmalate Dehydrogenase Gene of Candida UtilisMicrobiology, 1987
- Crystallographic R Factor Refinement by Molecular DynamicsScience, 1987
- PRINCIPLES THAT DETERMINE THE STRUCTURE OF PROTEINSAnnual Review of Biochemistry, 1984
- Three-dimensional structure of glutathione reductase at 2 Å resolutionJournal of Molecular Biology, 1981
- Chemical and biological evolution of a nucleotide-binding proteinNature, 1974
- Polypeptide conformation of cytoplasmic malate dehydrogenase from an electron density map at 3.0 Å resolutionJournal of Molecular Biology, 1972
- Regulation of Isocitrate Dehydrogenase Activity in Escherichia coli on Adaptation to AcetateJournal of General Microbiology, 1971
- Synthesis of C4-dicarboxylic acids from acetate by a “glyoxylate bypass” of the tricarboxylic acid cycleBiochimica et Biophysica Acta, 1957