The molecular structure of the Na(+)-translocating F1F0-ATPase of Acetobacterium woodii, as revealed by electron microscopy, resembles that of H(+)-translocating ATPases.
The Na(+)-translocating F1F0-ATPase of Acetobacterium woodii was examined by electron microscopy. After reconstitution into proteoliposomes, knobs typical for the F1 domain were visible on the outside of the membrane. The F1-part of the isolated enzyme showed a hexagonal symmetry suggesting an alpha 3 beta 3 structure, and the F1F0 complex had molecular dimensions very similar to those of H(+)-translocating ATPases of E. coli, chloroplasts, and mitochondria.
Reidlinger
J
J
Institut für Mikrobiologie der Georg-August-Universität, Göttingen, Germany.
Mayer
F
F
Müller
V
V
D000251:Adenosine Triphosphatases / Q000648:ultrastructure*; D027682:Cation Transport Proteins; D006093:Gram-Positive Asporogenous Rods / Q000201:enzymology* / Q000648:ultrastructure; D006180:Proton-Translocating ATPases / Q000648:ultrastructure*; D012964:Sodium / Q000378:metabolism
D027682:Cation Transport Proteins; D012964:Sodium; D000251:Adenosine Triphosphatases; C021838:sodium-translocating ATPase; D006180:Proton-Translocating ATPases