title: Localization of the delta subunit in the Escherichia coli F(1)F(0)-ATPsynthase by immuno electron microscopy: the delta subunit binds on top of the F(1).
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.
authors.affiliation: Department of Biochemistry, University of California, Riverside, CA, 92521, USA. stephan.wilkens@ucr.edu
authors.forename: S
authors.initials: S
authors.lastname: Wilkens
authors.forename: J
authors.initials: J
authors.lastname: Zhou
authors.forename: R
authors.initials: R
authors.lastname: Nakayama
authors.forename: S D
authors.initials: SD
authors.lastname: Dunn
authors.forename: R A
authors.initials: RA
authors.lastname: Capaldi
mesh_terms: D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology*; D016253:Microscopy, Immunoelectron; D006180:Proton-Translocating ATPases / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D006180:Proton-Translocating ATPases