Solution structure of a C-terminal coiled-coil domain from bovine IF(1): the inhibitor protein of F(1) ATPase.
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.
Gordon-Smith
D J
DJ
MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK.
Carbajo
R J
RJ
Yang
J C
JC
Videler
H
H
Runswick
M J
MJ
Walker
J E
JE
Neuhaus
D
D
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D019281:Dimerization; D006639:Histidine / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors*; D012996:Solutions; D013816:Thermodynamics; D000097795:ATPase Inhibitory Protein
D006639:Histidine; D010446:Peptide Fragments; D011506:Proteins; D006180:Proton-Translocating ATPases; D012996:Solutions; D000097795:ATPase Inhibitory Protein