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TitleSubnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase.
Journal, issue, pagesNature, Vol. 481, Issue 7380, Page 214-218, Year 2011
Publish dateDec 18, 2011
AuthorsWilson C Y Lau / John L Rubinstein /
PubMed AbstractIon-translocating rotary ATPases serve either as ATP synthases, using energy from a transmembrane ion motive force to create the cell's supply of ATP, or as transmembrane ion pumps that are powered ...Ion-translocating rotary ATPases serve either as ATP synthases, using energy from a transmembrane ion motive force to create the cell's supply of ATP, or as transmembrane ion pumps that are powered by ATP hydrolysis. The members of this family of enzymes each contain two rotary motors: one that couples ion translocation to rotation and one that couples rotation to ATP synthesis or hydrolysis. During ATP synthesis, ion translocation through the membrane-bound region of the complex causes rotation of a central rotor that drives conformational changes and ATP synthesis in the catalytic region of the complex. There are no structural models available for the intact membrane region of any ion-translocating rotary ATPase. Here we present a 9.7 Å resolution map of the H(+)-driven ATP synthase from Thermus thermophilus obtained by electron cryomicroscopy of single particles in ice. The 600-kilodalton complex has an overall subunit composition of A(3)B(3)CDE(2)FG(2)IL(12). The membrane-bound motor consists of a ring of L subunits and the carboxy-terminal region of subunit I, which are equivalent to the c and a subunits of most other rotary ATPases, respectively. The map shows that the ring contains 12 L subunits and that the I subunit has eight transmembrane helices. The L(12) ring and I subunit have a surprisingly small contact area in the middle of the membrane, with helices from the I subunit making contacts with two different L subunits. The transmembrane helices of subunit I form bundles that could serve as half-channels across the membrane, with the first half-channel conducting protons from the periplasm to the L(12) ring and the second half-channel conducting protons from the L(12) ring to the cytoplasm. This structure therefore suggests the mechanism by which a transmembrane proton motive force is converted to rotation in rotary ATPases.
External linksNature / PubMed:22178924
MethodsEM (single particle)
Resolution9.7 Å
Structure data

5335

3j0j

EMDB-5335: Sub-nanometer resolution structure of the intact T. thermophilus proton-driven ATP synthase reveals the arrangement of its trans-membrane helices
PDB-3j0j: Fitted atomic models of Thermus thermophilus V-ATPase subunits into cryo-EM map
Method: EM (single particle) / Resolution: 9.7 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • Thermus thermophilus HB8 (bacteria)
  • thermus thermophilus (bacteria)
KeywordsHYDROLASE / flexible fitting / rigid body fitting / membrane protein complex

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