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	Engineering of ATP synthase for enhancement of proton-to-ATP ratio.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 5410, Year 2025
Publish date	Jul 3, 2025
Authors	Hiroshi Ueno / Kiyoto Yasuda / Norie Hamaguchi-Suzuki / Riku Marui / Naruhiko Adachi / Toshiya Senda / Takeshi Murata / Hiroyuki Noji /
PubMed Abstract	FF-ATP synthase (FF) interconverts the energy of the proton motive force (pmf) and that of ATP through the mechanical rotation. The H/ATP ratio, one of the most crucial parameters in bioenergetics, ...FF-ATP synthase (FF) interconverts the energy of the proton motive force (pmf) and that of ATP through the mechanical rotation. The H/ATP ratio, one of the most crucial parameters in bioenergetics, varies among species due to differences in the number of H-binding c-subunits, resulting in H/ATP ratios ranging from 2.7 to 5. In this study, we seek to significantly enhance the H/ATP ratio by employing an alternative approach that differs from that of nature. We engineer FF to form multiple peripheral stalks, each bound to a proton-conducting a-subunit. The engineered FF exhibits an H/ATP ratio of 5.8, surpassing the highest ratios found in naturally occurring FFs, enabling ATP synthesis under low pmf conditions where wild-type enzymes cannot synthesize ATP. Structural analysis reveals that the engineered FF forms up to three peripheral stalks and a-subunits. This study not only provides valuable insights into the H-transport mechanism of FF but also opens up possibilities for engineering the foundation of cellular bioenergetics.
External links	Nat Commun / PubMed:40610443 / PubMed Central
Methods	EM (single particle)
Resolution	2.54 - 6.59 Å
Structure data	61339 9jc1 EMDB-61339, PDB-9jc1: Engineering of ATP synthase Method: EM (single particle) / Resolution: 2.79 Å 61340 9jc2 EMDB-61340, PDB-9jc2: Engineering of ATP synthase Fo Method: EM (single particle) / Resolution: 3.96 Å EMDB-61341: Engineering of ATP synthase single stalk1 Method: EM (single particle) / Resolution: 2.54 Å EMDB-61342: Engineering of ATP synthase single stalk2 Method: EM (single particle) / Resolution: 2.64 Å EMDB-61343: Engineering of ATP synthase single stalk3 Method: EM (single particle) / Resolution: 2.98 Å EMDB-61344: Engineering of ATP synthase Double stalks1,2 Method: EM (single particle) / Resolution: 2.67 Å EMDB-61345: Engineering of ATP synthase Double stalks1,3 Method: EM (single particle) / Resolution: 3.23 Å EMDB-61346: Engineering of ATP synthase Double stalks2,3 Method: EM (single particle) / Resolution: 2.99 Å EMDB-61347: Engineering of ATP synthase Zero stalk Method: EM (single particle) / Resolution: 2.62 Å EMDB-61348: Engineering of ATP synthase single stalk1 Fo Method: EM (single particle) / Resolution: 3.86 Å EMDB-61349: Engineering of ATP synthase single stalk2 Fo Method: EM (single particle) / Resolution: 3.48 Å EMDB-61350: Engineering of ATP synthase single stalk3 Fo Method: EM (single particle) / Resolution: 5.63 Å EMDB-61351: Engineering of ATP synthase Double stalks1,2 Fo Method: EM (single particle) / Resolution: 3.62 Å EMDB-61352: Engineering of ATP synthase Double stalks1,3 Fo Method: EM (single particle) / Resolution: 6.59 Å EMDB-61353: Engineering of ATP synthase Double stalks2,3 Fo Method: EM (single particle) / Resolution: 4.69 Å EMDB-61354: Engineering of ATP synthase Zero stalk Fo Method: EM (single particle) / Resolution: 3.86 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-MG*: Unknown entry
Source	bacillus sp. ps3 (bacteria)
Keywords	MEMBRANE PROTEIN / Molecular Motor / ATP synthase