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The Oligomeric Subunit c Rotor in the Fo Sector of ATP Synthase: Unresolved Questions in Our Understanding of Function
Authors:Robert H Fillingame  Weiping Jiang  Oleg Y Dmitriev
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
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.
Keywords:FoF1-ATP synthase  Fo rotary motor  subunit c  subunit a  transmembrane helices  NMR  cross linking
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