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Title | Three-dimensional structure of the intact Thermus thermophilus H+-ATPase/synthase by electron microscopy. |
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Journal, issue, pages | Structure, Vol. 12, Issue 10, Page 1789-1798, Year 2004 |
Publish date | Mar 14, 2005 |
Authors | Ricardo A Bernal / Daniela Stock / |
PubMed Abstract | 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 ...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 links | Structure / PubMed:15458628 |
Methods | EM (single particle) |
Resolution | 23.0 Å |
Structure data | EMDB-5301: |
Source |
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