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PMID: 2682654 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.

Hurley JH, Thorsness PE, Ramalingam V, Helmers NH, Koshland DE, Stroud RM

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.

MeSH Terms
3-Isopropylmalate Dehydrogenase Alcohol Oxidoreductases/genetics Amino Acid Sequence Escherichia coli/enzymology Homeostasis Isocitrate Dehydrogenase/genetics,metabolism Models, Molecular Molecular Sequence Data Phosphorylation Protein Conformation Sequence Homology, Nucleic Acid
Chemicals
Alcohol Oxidoreductases Isocitrate Dehydrogenase 3-Isopropylmalate Dehydrogenase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Hurley J H
Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.
Thorsness P E
Ramalingam V
Helmers N H
Koshland D E
Stroud R M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1989-11-00
Pages
8635-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC298342
Subset
IM
Grants
NIGMS NIH HHS · GM 24485 · United States
Databases
PDB
Analysis Services
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