Three-dimensional Structure of A1A0 ATP Synthase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Electron MicroscopyS

• Published in: The Journal of biological chemistry Vol. 284; no. 15; pp. 10110 - 10119
• Main Authors: Vonck, Janet, Pisa, Kim Y., Morgner, Nina, Brutschy, Bernhard, Müller, Volker
• Format: Journal Article
• Language: English
• Published: American Society for Biochemistry and Molecular Biology 10.04.2009
• Subjects: Glycobiology and Extracellular Matrices
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M808498200

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 .