Cargando…
Structural basis of unisite catalysis of bacterial F(0)F(1)-ATPase
Adenosine triphosphate (ATP) synthases (F(0)F(1)-ATPases) are crucial for all aerobic organisms. F(1), a water-soluble domain, can catalyze both the synthesis and hydrolysis of ATP with the rotation of the central γε rotor inside a cylinder made of α(3)β(3) in three different conformations (referred...
Autores principales: | Nakano, Atsuki, Kishikawa, Jun-ichi, Nakanishi, Atsuko, Mitsuoka, Kaoru, Yokoyama, Ken |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9896953/ https://www.ncbi.nlm.nih.gov/pubmed/36741449 http://dx.doi.org/10.1093/pnasnexus/pgac116 |
Ejemplares similares
-
Cryo-EM studies of the rotary H(+)-ATPase/synthase from Thermus thermophilus
por: Nakanishi, Atsuko, et al.
Publicado: (2019) -
Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase
por: Nakano, Atsuki, et al.
Publicado: (2023) -
Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding
por: Nakanishi, Atsuko, et al.
Publicado: (2023) -
Cryo EM structure of intact rotary H(+)-ATPase/synthase from Thermus thermophilus
por: Nakanishi, Atsuko, et al.
Publicado: (2018) -
Mechanical inhibition of isolated V(o) from V/A-ATPase for proton conductance
por: Kishikawa, Jun-ichi, et al.
Publicado: (2020)