The gamma subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part.
A mutant, in which a cysteine has been site-directed into the polar loop region of the c subunit at residue 44, has been studied. Cross-linking of the c subunit to both the gamma and epsilon subunits was observed with cupric 1,10-phenanthrolinate treatment. The linkage between the c and gamma subunits was localized to that part of the gamma subunit between residues 202-286, based on peptide analysis. Reference to the high resolution structure of F1 [Abrahams et al. (1994) Nature 370, 621-628] appears to limit this contact site to the region including residues 202-230. This segment contains 4 tyrosines and 1 tryptophan as possible reactive residues for cross-linking with the c subunit cysteine.
Watts
S D
SD
Institute of Molecular Biology, University of Oregon, Eugene 97403, USA.
Zhang
Y
Y
Fillingame
R H
RH
Capaldi
R A
RA
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D003432:Cross-Linking Reagents; D003545:Cysteine / Q000378:metabolism; D004220:Disulfides; D004926:Escherichia coli / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009154:Mutation; D010618:Phenanthrolines; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D003432:Cross-Linking Reagents; D004220:Disulfides; D010618:Phenanthrolines; C014741:bis(1,10-phenanthroline)copper(2+) ion; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases; D003545:Cysteine