Topographical structure of membrane‐bound Escherichia coli F1F0 ATP synthase in aqueous buffer

FEBS Letters

Bustamante, Carlos J.²  Turina, Paola³  Capaldi, Roderick³  Keller, David J.¹  Singh, Seema¹ 

[1] Department of Chemistry, University of New Mexico, Albuquerque, NM 87131, USA;Institute of Molecular Biology, Howard Hughes Medical Institute, University of Oregon, Eugene, OR 97403-1229, USA;Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, USA

关键词: ATP synthase;    Scanning force microscopy;    Atomic force microscopy;    Tapping mode;    Membrane protein;   

DOI  :  10.1016/S0014-5793(96)01127-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Scanning force microscope images of membrane-bound Escherichia coli ATP synthase F₀ complexes have been obtained in aqueous solution. The images show a consistent set of internal features: a ring structure which surrounds a central dimple and contains an asymmetric lateral mass. Images of trypsin-treated F₀ complexes, which have lost part of their b subunits, show a reduced asymmetric mass, while images of c-subunit oligomers, which lack both the a and b subunits, show a ring and dimple but do not have an asymmetric mass. These results support models in which the F₀ complex contains a ring of 9–12 c subunits with the b subunits located outside this ring, and show that scanning force microscopy is able to provide structural information on membrane proteins of molecular mass less than 200 000 Da.

【 授权许可】

Unknown