A cryoelectron microscopy study of the interaction of the Escherichia coli F1-ATPase with subunit b dimer.
A complex between the Escherichia coli F1-ATPase and a truncated form of the ECF0-b subunit was formed and examined by cryoelectron microscopy in amorphous ice. Image analysis of single particles in the hexagonal projection revealed that the polar domain of the b subunit interacts with a beta subunit different from the one which interacts with the epsilon subunit. The cavity in the enzyme, visible in the hexagonal projection, is not filled by the b polypeptide, therefore leaving enough room for extensive conformational changes of the gamma and epsilon subunits within the native F1F0 complex.
Institute of Molecular Biology, University of Oregon, Eugene 97403.
S
S
Wilkens
S D
SD
Dunn
R A
RA
Capaldi
D000595:Amino Acid Sequence; D015925:Cryopreservation; D004926:Escherichia coli / Q000201:enzymology*; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D017386:Sequence Homology, Amino Acid
D006180:Proton-Translocating ATPases