6f36

Polytomella Fo modelPolytomella Fo model

6f36, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Structural highlights 6f36 is a 12 chain structure with sequence from Polytomella sp. pringsheim 198.80. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Structural basis of proton translocation and force generation in mitochondrial ATP synthase.,Klusch N, Murphy BJ, Mills DJ, Yildiz O, Kuhlbrandt W Elife. 2017 Dec 6;6. doi: 10.7554/eLife.33274. PMID:29210357 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.