ATP5F1B cDNA ORF clone, Bos taurus(cattle)

Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.
Zhou A, Rohou A, Schep DG, Bason JV, Montgomery MG, Walker JE, Grigorieff N, Rubinstein JL
eLife4e10180(2015 Oct)

Effects of an ATP analogue, adenosine 5'-[?-thio]-triphosphate, on F1-ATPase rotary catalysis, torque generation, and inhibited intermediated formation.
Yukawa A, Watanabe R, Noji H
Biochemical and biophysical research communications458(3)515-9(2015 Mar)

Rotation triggers nucleotide-independent conformational transition of the empty ? subunit of F?-ATPase.
Czub J, Grubm?ller H
Journal of the American Chemical Society136(19)6960-8(2014 May)

Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria.
Rees DM, Montgomery MG, Leslie AG, Walker JE
Proceedings of the National Academy of Sciences of the United States of America109(28)11139-43(2012 Jul)

Domain motion of individual F1-ATPase ?-subunits during unbiased molecular dynamics simulations.
Kleinekath?fer U, Isralewitz B, Dittrich M, Schulten K
The journal of physical chemistry. A115(25)7267-74(2011 Jun)

Combining cryoelectron microscopy data with bioinformatic analysis allowed the authors to determine the fold of the a subunit, suggesting a proton translocation path through the FO region that involves both the a and b subunits.
Title: Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.

These data indicate that interaction with the alpha-phosphate is not crucial for efficient catalysis, but likely contributes to avoid formation of ADP-inhibited intermediates.
Title: Effects of an ATP analogue, adenosine 5'-[?-thio]-triphosphate, on F1-ATPase rotary catalysis, torque generation, and inhibited intermediated formation.

Molecular dynamics simulations show that the nucleotide-free beta subunit, initially in the open, low-affinity state, undergoes a spontaneous closing transition to the half-open state in response to the gamma rotation in the synthesis direction.
Title: Rotation triggers nucleotide-independent conformational transition of the empty ? subunit of F?-ATPase.

analysis of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria
Title: Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria.

Molecular dynamics simulations of F1-ATPase suggest that the equilibrium conformation of a nucleotide-free beta-subunit is the open conformation and that the transition from the closed to the open conformation can occur in a few tens of nanoseconds.
Title: Domain motion of individual F1-ATPase ?-subunits during unbiased molecular dynamics simulations.