Molecular architecture of Manduca sexta midgut V1 ATPase visualized by electron microscopy.
The structure of the V1 ATPase from the tobacco hornworm Manduca sexta has been determined from electron micrographs of isolated, negatively stained specimens. The resulting images clearly show a pseudohexagonal arrangement of six equal-sized protein densities, presumably representing the three copies each of subunits A and B, which comprise the headpiece of the enzyme. A seventh density could be observed either centrally or asymmetrically to the hexamer. The maximum diameter of the V1 complex in the hexagonal projection is 13 nm with each of the six peripheral densities being 3-4 nm in diameter.
Radermacher
M
M
Max-Planck-Institut für Biophysik, Abteilung Strukturbiologie, Frankfurt am Main, Germany.
Ruiz
T
T
Harvey
W R
WR
Wieczorek
H
H
Grüber
G
G
D000818:Animals; D004064:Digestive System / Q000201:enzymology*; D007091:Image Processing, Computer-Assisted; D018402:Manduca / Q000201:enzymology*; D008854:Microscopy, Electron; D006180:Proton-Translocating ATPases / Q000648:ultrastructure*; D025262:Vacuolar Proton-Translocating ATPases
D025262:Vacuolar Proton-Translocating ATPases; D006180:Proton-Translocating ATPases