Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure of the human ATP synthase.
Journal, issue, pages	Mol Cell, Vol. 83, Issue 12, Page 2137-22147.e4, Year 2023
Publish date	Jun 15, 2023
Authors	Yuezheng Lai / Yuying Zhang / Shan Zhou / Jinxu Xu / Zhanqiang Du / Ziyan Feng / Long Yu / Ziqing Zhao / Weiwei Wang / Yanting Tang / Xiuna Yang / Luke W Guddat / Fengjiang Liu / Yan Gao / Zihe Rao / Hongri Gong /
PubMed Abstract	Biological energy currency ATP is produced by FF-ATP synthase. However, the molecular mechanism for human ATP synthase action remains unknown. Here, we present snapshot images for three main ...Biological energy currency ATP is produced by FF-ATP synthase. However, the molecular mechanism for human ATP synthase action remains unknown. Here, we present snapshot images for three main rotational states and one substate of human ATP synthase using cryoelectron microscopy. These structures reveal that the release of ADP occurs when the β subunit of FF-ATP synthase is in the open conformation, showing how ADP binding is coordinated during synthesis. The accommodation of the symmetry mismatch between F and F motors is resolved by the torsional flexing of the entire complex, especially the γ subunit, and the rotational substep of the c subunit. Water molecules are identified in the inlet and outlet half-channels, suggesting that the proton transfer in these two half-channels proceed via a Grotthus mechanism. Clinically relevant mutations are mapped to the structure, showing that they are mainly located at the subunit-subunit interfaces, thus causing instability of the complex.
External links	Mol Cell / PubMed:37244256
Methods	EM (single particle)
Resolution	2.53 - 8.0 Å
Structure data	34564 8h9e EMDB-34564, PDB-8h9e: Human ATP synthase F1 domain, state 1 Method: EM (single particle) / Resolution: 2.53 Å 34565 8h9f EMDB-34565, PDB-8h9f: Human ATP synthase state 1 subregion 3 Method: EM (single particle) / Resolution: 2.69 Å 34566 8h9g EMDB-34566, PDB-8h9g: Human ATP synthase state 1 subregion 2 Method: EM (single particle) / Resolution: 2.95 Å 34568 8h9i EMDB-34568, PDB-8h9i: Human ATP synthase F1 domain, state2 Method: EM (single particle) / Resolution: 2.77 Å 34569 8h9j EMDB-34569, PDB-8h9j: Human ATP synthase state2 subregion 3 Method: EM (single particle) / Resolution: 3.26 Å 34570 8h9k EMDB-34570, PDB-8h9k: Human ATP synthase state 2 subregion 2 Method: EM (single particle) / Resolution: 3.51 Å 34572 8h9l EMDB-34572, PDB-8h9l: Human ATP synthase F1 domain, state 3a Method: EM (single particle) / Resolution: 2.61 Å 34573 8h9m EMDB-34573, PDB-8h9m: Human ATP synthase state 3a subregion 3 Method: EM (single particle) / Resolution: 3.0 Å 34574 8h9n EMDB-34574, PDB-8h9n: Human ATP synthase state 3a subregion 2 Method: EM (single particle) / Resolution: 3.56 Å 34576 8h9p EMDB-34576, PDB-8h9p: Human ATP synthase F1 domain, state 3b Method: EM (single particle) / Resolution: 3.02 Å 34577 8h9q EMDB-34577, PDB-8h9q: Human ATP synthase state 3b subregion 3 Method: EM (single particle) / Resolution: 3.47 Å 34578 8h9r EMDB-34578, PDB-8h9r: Human ATP synthase state 3b subregion 2 Method: EM (single particle) / Resolution: 3.97 Å 34580 8h9s EMDB-34580, PDB-8h9s: Human ATP synthase state 1 (combined) Method: EM (single particle) / Resolution: 2.53 Å 34581 8h9t EMDB-34581, PDB-8h9t: Human ATP synthase state 2 (combined) Method: EM (single particle) / Resolution: 2.77 Å 34582 8h9u EMDB-34582, PDB-8h9u: Human ATP synthase state 3a (combined) Method: EM (single particle) / Resolution: 2.61 Å 34583 8h9v EMDB-34583, PDB-8h9v: Human ATP synthase state 3b (combined) Method: EM (single particle) / Resolution: 3.02 Å EMDB-34584: Human ATP synthase dimer Method: EM (single particle) / Resolution: 8.0 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-CDL: CARDIOLIPIN / phospholipidYM / Cardiolipin ChemComp-3PH*: 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE / Phosphatidic acid
Source	homo sapiens (human) human (human)
Keywords	MEMBRANE PROTEIN / ATP synthase