Klusch 2017 Elife

Has title::Klusch N, Murphy BJ, Mills DJ, Yildiz Ö, Kühlbrandt W (2017) Structural basis of proton translocation and force generation in mitochondrial ATP synthase. Elife e33274. doi: 10.7554/eLife.33274.

» [[Has info::PMID: 29210357 Open Access]]

Was written by::Klusch N, Was written by::Murphy BJ, Was written by::Mills DJ, Was written by::Yildiz O, Was written by::Kuehlbrandt W (Was published in year::2017) Was published in journal::Elife

Abstract: [[has abstract::ATP synthases produce ATP by rotary catalysis, powered by the electrochemical proton gradient across the membrane. Understanding this fundamental process requires an atomic model of the proton pathway. We determined the structure of an intact mitochondrial ATP synthase dimer by electron cryo-microscopy at near-atomic resolution. Charged and polar residues of the a-subunit stator define two aqueous channels, each spanning one half of the membrane. Passing through a conserved membrane-intrinsic helix hairpin, the lumenal channel protonates an acidic glutamate in the c-ring rotor. Upon ring rotation, the protonated glutamate encounters the matrix channel and deprotonates. An arginine between the two channels prevents proton leakage. The steep potential gradient over the sub-nm inter-channel distance exerts a force on the deprotonated glutamate, resulting in net directional rotation.]] • Keywords: has publicationkeywords::ATP synthase; biochemistry; biophysics; electron cryo-microscopy; energy conversion; membrane potential; membrane protein structure; mitochondria; structural biology • Bioblast editor: [[has editor::Gnaiger E]]

Labels:

Enzyme: Enzyme::Complex V;ATP synthase  Regulation: Topic::Coupling efficiency;uncoupling, Topic::mt-Membrane potential 

additional label::BEC 2020.2