ATP synthase: constrained stoichiometry of the transmembrane rotor

FEBS Letters

Matthey, Ulrich³  Stahlberg, Henning¹  Suda, Kitaru¹  Dimroth, Peter³  Dencher, Norbert A.⁴  Meier, Thomas³  Engel, Andreas¹  Seelert, Holger⁴  Müller, Daniel J.² 

[1] M.E. Müller-Institute for Structural Biology, Biozentrum, University of Basel, CH-4056 Basel, Switzerland;Max-Planck-Institute of Molecular Cell Biology and Genetics, D-01307 Dresden, Germany;Institute of Microbiology, Eidgenössische Technische Hochschule (ETH), CH-8092 Zurich, Switzerland;Physical Biochemistry, Department of Chemistry, Darmstadt University of Technology, D-64287 Darmstadt, Germany

关键词: Atomic force microscopy;    ATP synthase;    Structural assembly;    Molecular interaction;    AFM;    atomic force microscopy;    ATP;    adenosine triphosphate;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/S0014-5793(01)02708-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recent structural data suggest that the number of identical subunits (c or III) assembled into the cation-powered rotor of F₁F₀ ATP synthase depends on the biological origin. Atomic force microscopy allowed individual subunits of the cylindrical transmembrane rotors from spinach chloroplast and from Ilyobacter tartaricus ATP synthase to be directly visualized in their native-like environment. Occasionally, individual rotors exhibit structural gaps of the size of one or more subunits. Complete rotors and arch-shaped fragments of incomplete rotors revealed the same diameter within one ATP synthase species. These results suggest the rotor diameter and stoichiometry to be determined by the shape of the subunits and their nearest neighbor interactions.

【 授权许可】

Unknown