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TitleRotary mechanism of the prokaryotic V motor driven by proton motive force.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 9883, Year 2024
Publish dateNov 20, 2024
AuthorsJun-Ichi Kishikawa / Yui Nishida / Atsuki Nakano / Takayuki Kato / Kaoru Mitsuoka / Kei-Ichi Okazaki / Ken Yokoyama /
PubMed AbstractATP synthases play a crucial role in energy production by utilizing the proton motive force (pmf) across the membrane to rotate their membrane-embedded rotor c-ring, and thus driving ATP synthesis in ...ATP synthases play a crucial role in energy production by utilizing the proton motive force (pmf) across the membrane to rotate their membrane-embedded rotor c-ring, and thus driving ATP synthesis in the hydrophilic catalytic hexamer. However, the mechanism of how pmf converts into c-ring rotation remains unclear. This study presents a 2.8 Å cryo-EM structure of the V domain of V/A-ATPase from Thermus thermophilus, revealing precise orientations of glutamate (Glu) residues in the c-ring. Three Glu residues face a water channel, with one forming a salt bridge with the Arginine in the stator (a/Arg). Molecular dynamics (MD) simulations show that protonation of specific Glu residues triggers unidirectional Brownian motion of the c-ring towards ATP synthesis. When the key Glu remains unprotonated, the salt bridge persists, blocking rotation. These findings suggest that asymmetry in the protonation of c/Glu residues biases c-ring movement, facilitating rotation and ATP synthesis.
External linksNat Commun / PubMed:39567487 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.6 Å
Structure data

39644

8ywt

EMDB-39644, PDB-8ywt:
The isolated Vo domain of V/A-ATPase from Thermus thermophilus.
Method: EM (single particle) / Resolution: 2.8 Å

39661

8yxz

EMDB-39661, PDB-8yxz:
Vo domain of V/A-ATPase from Thermus thermophilus state1
Method: EM (single particle) / Resolution: 3.0 Å

39662

8yy0

EMDB-39662, PDB-8yy0:
Vo domain of V/A-ATPase from Thermus thermophilus state2
Method: EM (single particle) / Resolution: 3.6 Å

39663

8yy1

EMDB-39663, PDB-8yy1:
Vo domain of V/A-ATPase from Thermus thermophilus state3
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • thermus thermophilus hb8 (bacteria)
KeywordsMOTOR PROTEIN / ROTARY ATPASE / V/A-ATPASE / MOLECULAR MOTOR / ATP synthase

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