Abstract:
:Conformational changes within the subunit b-dimer of the E. coli ATP synthase occur upon binding to the F(1) sector. ESR spectra of spin-labeled b at room temperature indicated a pivotal point in the b-structure at residue 62. Spectra of frozen b +/- F(1) and calculated interspin distances suggested that where contact between b (2) and F(1) occurs (above about residue 80), the structure of the dimer changes minimally. Between b-residues 33 and 64 inter-subunit distances in the F(1)-bound b-dimer were found to be too large to accommodate tightly coiled coil packing and therefore suggest a dissociation and disengagement of the dimer upon F(1)-binding. Mechanistic implications of this "bubble" formation in the tether domain of ATP synthase b ( 2 ) are discussed.
journal_name
J Bioenerg Biomembrjournal_title
Journal of bioenergetics and biomembranesauthors
Zaida TM,Hornung T,Volkov OA,Hoffman AD,Pandey SJ,Wise JG,Vogel PDdoi
10.1007/s10863-008-9189-zsubject
Has Abstractpub_date
2008-12-01 00:00:00pages
551-9issue
6eissn
0145-479Xissn
1573-6881journal_volume
40pub_type
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