FEBS Letters | |
Topographical structure of membrane‐bound Escherichia coli F1F0 ATP synthase in aqueous buffer | |
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
【 预 览 】
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RO201912020303489ZK.pdf | 483KB | download |