| Literature DB >> 10623533 |
S Wilkens1, J Zhou, R Nakayama, S D Dunn, R A Capaldi.
Abstract
The binding site of the delta subunit in the F(1)F(0)-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 on the F(1) despite there being three identical alphabeta 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. Copyright 2000 Academic Press.Entities:
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Year: 2000 PMID: 10623533 DOI: 10.1006/jmbi.1999.3381
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469