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The Torque of Rotary F-ATPase Can Unfold Subunit Gamma If Rotor and Stator Are Cross-Linked

During ATP hydrolysis by F(1)-ATPase subunit γ rotates in a hydrophobic bearing, formed by the N-terminal ends of the stator subunits (αβ)(3). If the penultimate residue at the α-helical C-terminal end of subunit γ is artificially cross-linked (via an engineered disulfide bridge) with the bearing, t...

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Detalles Bibliográficos
Autores principales: Hilbers, Florian, Junge, Wolfgang, Sielaff, Hendrik
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3536650/
https://www.ncbi.nlm.nih.gov/pubmed/23301103
http://dx.doi.org/10.1371/journal.pone.0053754