PMID:10838050

Citation	Dunn, SD, McLachlin, DT and Revington, M (2000) The second stalk of Escherichia coli ATP synthase. Biochim. Biophys. Acta 1458:356-63
Abstract	Two stalks link the F(1) and F(0) sectors of ATP synthase. The central stalk contains the gamma and epsilon subunits and is thought to function in rotational catalysis as a rotor driving conformational changes in the catalytic alpha(3)beta(3) complex. The two b subunits and the delta subunit associate to form b(2)delta, a second, peripheral stalk extending from the membrane up the side of alpha(3)beta(3) and binding to the N-terminal regions of the alpha subunits, which are approx. 125 A from the membrane. This second stalk is essential for binding F(1) to F(0) and is believed to function as a stator during rotational catalysis. In vitro, b(2)delta is a highly extended complex held together by weak interactions. Recent work has identified the domains of b which are essential for dimerization and for interaction with delta. Disulphide cross-linking studies imply that the second stalk is a permanent structure which remains associated with one alpha subunit or alphabeta pair. However, the weak interactions between the polypeptides in b(2)delta pose a challenge for the proposed stator function.
Links	PubMed
Keywords	ATP Synthetase Complexes; Dimerization; Disulfides/chemistry; Escherichia coli/enzymology; Models, Molecular; Molecular Motor Proteins; Multienzyme Complexes/chemistry; Phosphotransferases (Phosphate Group Acceptor)/chemistry; Protein Binding; Protein Conformation; Proton-Translocating ATPases/chemistry
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