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-Structure paper
Title | Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy. |
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Journal, issue, pages | J Biol Chem, Vol. 284, Issue 15, Page 10110-10119, Year 2009 |
Publish date | Apr 10, 2009 |
![]() | Janet Vonck / Kim Y Pisa / Nina Morgner / Bernhard Brutschy / Volker Müller / ![]() |
PubMed Abstract | The archaeal ATP synthase is a multisubunit complex that consists of a catalytic A(1) part and a transmembrane, ion translocation domain A(0). The A(1)A(0) complex from the hyperthermophile ...The archaeal ATP synthase is a multisubunit complex that consists of a catalytic A(1) part and a transmembrane, ion translocation domain A(0). The A(1)A(0) complex from the hyperthermophile Pyrococcus furiosus was isolated. Mass analysis of the complex by laser-induced liquid bead ion desorption (LILBID) indicated a size of 730 +/- 10 kDa. A three-dimensional map was generated by electron microscopy from negatively stained images. The map at a resolution of 2.3 nm shows the A(1) and A(0) domain, connected by a central stalk and two peripheral stalks, one of which is connected to A(0), and both connected to A(1) via prominent knobs. X-ray structures of subunits from related proteins were fitted to the map. On the basis of the fitting and the LILBID analysis, a structural model is presented with the stoichiometry A(3)B(3)CDE(2)FH(2)ac(10). |
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Methods | EM (single particle) |
Resolution | 23.0 Å |
Structure data | ![]() EMDB-1542: |
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