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TitleThree-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy.
Journal, issue, pagesStructure, Vol. 12, Issue 10, Page 1789-1798, Year 2004
Publish dateMar 14, 2005
AuthorsRicardo A Bernal / Daniela Stock /
PubMed AbstractATPases are unique rotary motors that are essential to all living organisms because of their role in energy interconversion. A three-dimensional reconstruction of the intact H+-ATPase/synthase from ...ATPases are unique rotary motors that are essential to all living organisms because of their role in energy interconversion. A three-dimensional reconstruction of the intact H+-ATPase/synthase from Thermus thermophilus has revealed the presence of two interconnected peripheral stalks, a well-defined central stalk, and a hexagonally shaped hydrophobic domain. The peripheral stalks are each attached to the water soluble sector at a noncatalytic subunit interface and extend down toward the membrane where they interact with a strong elongated tube of density that runs parallel to the membrane and connects the two stalks. The central stalk is well resolved, especially with respect to its interaction with a single catalytic subunit giving rise to an asymmetry comparable to that identified in F-ATPases. The hexagonal shape of the membrane domain might suggest the presence of 12 proteolipids arranged as dimers, analogous to the proposed arrangement in the related eukaryotic V-ATPases.
External linksStructure / PubMed:15458628
MethodsEM (single particle)
Resolution23.0 Å
Structure data

EMDB-5301:
Negative Stain reconstruction of the Thermus thermophilus A-ATPase to 23 Angstrom. Opposite Hand to published.
Method: EM (single particle) / Resolution: 23.0 Å

Source
  • Thermus thermophilus (bacteria)

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