Three-dimensional structure of A1A0 ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy.
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).
Vonck
Janet
J
Max-Planck-Institute of Biophysics, Max-von-Laue-Strasse 3, D-60438 Frankfurt am Main, Germany. janet.vonck@mpibp-frankfurt.mpg.de
Pisa
Kim Y
KY
Morgner
Nina
N
Brutschy
Bernhard
B
Müller
Volker
V
D000255:Adenosine Triphosphate / Q000737:chemistry; D000595:Amino Acid Sequence; D001105:Archaea / Q000201:enzymology; D018360:Crystallography, X-Ray / Q000379:methods; D007477:Ions; D013058:Mass Spectrometry / Q000379:methods; D008854:Microscopy, Electron / Q000379:methods; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D020027:Pyrococcus furiosus / Q000201:enzymology*; D017386:Sequence Homology, Amino Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014357:Trypsin / Q000737:chemistry
D007477:Ions; D000255:Adenosine Triphosphate; D014357:Trypsin; D006180:Proton-Translocating ATPases