ATP synthase: subunit-subunit interactions in the stator stalk.
In ATP synthase, proton translocation through the Fo subcomplex and ATP synthesis/hydrolysis in the F1 subcomplex are coupled by subunit rotation. The static, non-rotating portions of F1 and Fo are attached to each other via the peripheral "stator stalk", which has to withstand elastic strain during subunit rotation. In Escherichia coli, the stator stalk consists of subunits b2delta; in other organisms, it has three or four different subunits. Recent advances in this area include affinity measurements between individual components of the stator stalk as well as a detailed analysis of the interaction between subunit delta (or its mitochondrial counterpart, the oligomycin-sensitivity conferring protein, OSCP) and F1. The current status of our knowledge of the structure of the stator stalk and of the interactions between its subunits will be discussed in this review.
Weber
Joachim
J
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409-1061, USA. joachim.weber@ttuhsc.edu
D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology*; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism*
D021122:Protein Subunits; D025261:Mitochondrial Proton-Translocating ATPases