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Localization of the δ subunit in the Escherichia coli F1F0-ATPsynthase by immune electron microscopy:: The subunit δ binds on top of the F1
被引:58
作者:
Wilkens, S
[1
]
Zhou, J
Nakayama, R
Dunn, SD
Capaldi, RA
机构:
[1] Univ Calif Riverside, Dept Biochem, Riverside, CA 92521 USA
[2] Univ Western Ontario, Dept Biochem, London, ON N6A 5C1, Canada
[3] Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA
关键词:
F1F0-ATPsynthase;
delta subunit;
second stalk;
electron microscopy;
D O I:
10.1006/jmbi.1999.3381
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
The binding site of the delta subunit in the F1F0-ATPsynthase from Escherichia coli has been determined by electron microscopy of negatively stained, antibody-decorated enzyme molecules. The images show that the antibody is bound at the very top of the F-1 domain indicating that at least part of delta is bound in the dimple formed by the N termini of the alpha and beta subunits. The data may explain why there is only one binding site for delta ore the F-1 despite there being three identical alpha beta pairs. The finding also implies that the b subunits of the F-0 have to extend all the way from the membrane surface to the very top of the F-1 domain to make contact with the delta subunit. (C) 2000 Academic Press.
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页码:387 / 391
页数:5
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