Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.

TitleSolution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.
Publication TypeJournal Article
Year of Publication2001
AuthorsGordon-Smith, DJ, Carbajo, RJ, Yang, JC, Videler, H, Runswick, MJ, Walker, JE, Neuhaus, D
JournalJ Mol Biol
Volume308
Issue2
Pagination325-39
Date Published2001 Apr 27
ISSN0022-2836
KeywordsAmino Acid Sequence, Animals, Binding Sites, Cattle, Dimerization, Histidine, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments, Protein Structure, Quaternary, Protein Structure, Tertiary, Proteins, Proton-Translocating ATPases, Solutions, Thermodynamics
Abstract

Bovine IF(1) is a basic, 84 amino acid residue protein that inhibits the hydrolytic action of the F(1)F(0) ATP synthase in mitochondria under anaerobic conditions. Its oligomerization state is dependent on pH. At a pH value below 6.5 it forms an active dimer. At higher pH values, two dimers associate to form an inactive tetramer. Here, we present the solution structure of a C-terminal fragment of IF(1) (44-84) containing all five of the histidine residues present in the sequence. Most unusually, the molecule forms an anti-parallel coiled-coil in which three of the five histidine residues occupy key positions at the dimer interface.

DOI10.1006/jmbi.2001.4570
Alternate JournalJ. Mol. Biol.
Citation Key10.1006/jmbi.2001.4570
PubMed ID11327770