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 ATP synthase from an early photosynthetic bacterium .
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 122, Issue 13, Page e2425824122, Year 2025
Publish date	Mar 25, 2025
Authors	Xin Zhang / Jingyi Wu / Zhenzhen Min / Jiamao Wang / Xin Hong / Xinkai Pei / Zihe Rao / Xiaoling Xu /
PubMed Abstract	F-type ATP synthase (FF) catalyzes proton motive force-driven ATP synthesis in mitochondria, chloroplasts, and bacteria. Different from the mitochondrial and bacterial enzymes, FF from photosynthetic ...F-type ATP synthase (FF) catalyzes proton motive force-driven ATP synthesis in mitochondria, chloroplasts, and bacteria. Different from the mitochondrial and bacterial enzymes, FF from photosynthetic organisms have evolved diverse structural and mechanistic details to adapt to the light-dependent reactions. Although complete structure of chloroplast FF has been reported, no high-resolution structure of an FF from photosynthetic bacteria has been available. Here, we report cryo-EM structures of an intact and functionally competent FF from (FF), a filamentous anoxygenic phototrophic bacterium from the earliest branch of photosynthetic organisms. The structures of FF in its ADP-free and ADP-bound forms for three rotational states reveal a previously unrecognized architecture of ATP synthases. A pair of peripheral stalks connect to the F head through a dimer of δ-subunits, and associate with two membrane-embedded a-subunits that are asymmetrically positioned outside and clamp F's c-ring. The two a-subunits constitute two proton inlets on the periplasmic side and two proton outlets on the cytoplasmic side, endowing FF with unique proton translocation pathways that allow more protons being translocated relative to single a-subunit FF. Our findings deepen understanding of the architecture and proton translocation mechanisms of FF synthases and suggest innovative strategies for modulating their activities by altering the number of a-subunit.
External links	Proc Natl Acad Sci U S A / PubMed:40131952 / PubMed Central
Methods	EM (single particle)
Resolution	2.84 - 5.18 Å
Structure data	60868 9itj EMDB-60868, PDB-9itj: Chloroflexus aurantiacus ATP synthase, state 1 Method: EM (single particle) / Resolution: 2.84 Å 60869 9itk EMDB-60869, PDB-9itk: Chloroflexus aurantiacus ATP synthase, state 2 Method: EM (single particle) / Resolution: 2.89 Å 60870 9itl EMDB-60870, PDB-9itl: Chloroflexus aurantiacus ATP synthase, state 3 Method: EM (single particle) / Resolution: 3.31 Å 60871 9itm EMDB-60871, PDB-9itm: Chloroflexus aurantiacus ATP synthase, state 1, focused refinement of FO Method: EM (single particle) / Resolution: 3.16 Å 60872 9itn EMDB-60872, PDB-9itn: Chloroflexus aurantiacus ATP synthase, state 1, focused refinement of FO and peripheral stalk Method: EM (single particle) / Resolution: 3.48 Å 60873 9ito EMDB-60873, PDB-9ito: Chloroflexus aurantiacus ATP synthase, state 2, focused refinement of FO Method: EM (single particle) / Resolution: 3.3 Å 60874 9itp EMDB-60874, PDB-9itp: Chloroflexus aurantiacus ATP synthase, state 2, focused refinement of FO and peripheral stalk Method: EM (single particle) / Resolution: 3.85 Å 60875 9itq EMDB-60875, PDB-9itq: Chloroflexus aurantiacus ATP synthase, state 3, focused refinement of FO Method: EM (single particle) / Resolution: 3.98 Å 60876 9itr EMDB-60876, PDB-9itr: Chloroflexus aurantiacus ATP synthase, state 3, focused refinement of FO and peripheral stalk Method: EM (single particle) / Resolution: 4.6 Å 60877 9its EMDB-60877, PDB-9its: Chloroflexus aurantiacus ADP-bound ATP synthase, state 1 Method: EM (single particle) / Resolution: 2.89 Å 60878 9itt EMDB-60878, PDB-9itt: Chloroflexus aurantiacus ADP-bound ATP synthase, state 2 Method: EM (single particle) / Resolution: 2.96 Å 60879 9itu EMDB-60879, PDB-9itu: Chloroflexus aurantiacus ADP-bound ATP synthase, state 3 Method: EM (single particle) / Resolution: 3.18 Å 60880 9itv EMDB-60880, PDB-9itv: Chloroflexus aurantiacus ADP-bound ATP synthase, state 1, focused refinement of FO Method: EM (single particle) / Resolution: 3.97 Å 60881 9itw EMDB-60881, PDB-9itw: Chloroflexus aurantiacus ADP-bound ATP synthase, state 1, focused refinement of FO and peripheral stalk Method: EM (single particle) / Resolution: 4.08 Å 60882 9itx EMDB-60882, PDB-9itx: Chloroflexus aurantiacus ADP-bound ATP synthase, state 2, focused refinement of FO Method: EM (single particle) / Resolution: 4.1 Å 60883 9ity EMDB-60883, PDB-9ity: Chloroflexus aurantiacus ADP-bound ATP synthase, state 2, focused refinement of FO and peripheral stalk Method: EM (single particle) / Resolution: 4.95 Å 60884 9itz EMDB-60884, PDB-9itz: Chloroflexus aurantiacus ADP-bound ATP synthase, state 3, focused refinement of FO Method: EM (single particle) / Resolution: 4.28 Å 60885 9iu0 EMDB-60885, PDB-9iu0: Chloroflexus aurantiacus ADP-bound ATP synthase, state 3, focused refinement of FO and peripheral stalk Method: EM (single particle) / Resolution: 5.18 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-PO4: PHOSPHATE ION
Source	chloroflexus aurantiacus j-10-fl (bacteria)
Keywords	MEMBRANE PROTEIN / ATP synthesis / proton channels / proton-motive force / proton translocation