The Oligomeric Subunit c Rotor in the Fo Sector of ATP Synthase: Unresolved Questions in Our Understanding of Function |
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Authors: | Robert H Fillingame Weiping Jiang Oleg Y Dmitriev |
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Institution: | (1) Department of Biomolecular Chemistry, University of Wisconsin Medical School, 1300 University avenue, Madison, Wisconsin, 53706;(2) Department of Biomolecular Chemistry, University of Wisconsin Medical School, 1300 University avenue, Madison, Wisconsin, 53706 |
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Abstract: | We have proposed a model for the oligomeric c-rotor of the Fo sector of ATP synthase and its interaction with subunit a during H+-transport driven rotation. The model is based upon the solution structure of monomeric subunit c, determined by NMR, and an extensive series of cross-linking distance constraints between c subunits and between subunits c and a. To explain the complete set of cross-linking data, we have suggested that the second transmembrane helix rotates during its interaction with subunit a in the course of the H+-translocation cycle. The H+-transport coupled rotation of this helix is proposed to drive the stepwise movement of the c-oligomeric rotor. The model is testable and provides a useful framework for addressing questions raised by other experiments. |
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Keywords: | FoF1-ATP synthase Fo rotary motor subunit c subunit a transmembrane helices NMR cross linking |
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