Identification of aqueous access residues of the sodium half channel in transmembrane helix 5 of the Fo-a subunit of Propionigenium modestum ATP synthase

@article{Mitome2017IdentificationOA,
  title={Identification of aqueous access residues of the sodium half channel in transmembrane helix 5 of the Fo-a subunit of Propionigenium modestum ATP synthase},
  author={Noriyo Mitome and Hiroki Sato and Taishi Tomiyama and Katsuya Shimabukuro and Takuya Matsunishi and Kohei Hamada and Toshiharu Suzuki},
  journal={Biophysics and Physicobiology},
  year={2017},
  volume={14},
  pages={41 - 47}
}
The Fo-a subunit of the Na+-transporting FoF1 ATP synthase from Propionigenium modestum plays a key role in Na+ transport. It forms half channels that allow Na+ to enter and leave the buried carboxyl group on Fo-c subunits. The essential Arg residue R226, which faces the carboxyl group of Fo-c subunits in the middle of transmembrane helix 5 of the Fo-a subunit, separates the cytoplasmic side and periplasmic half-channels. To elucidate contributions of other amino acid residues of transmembrane… 
4 Citations

Characterizing the Hydration Properties of Proton Binding Sites in the ATP Synthase C-Rings of Bacillus Species.

The data suggest that a water molecule stably binds to the P51A mutant of BacillusPS3, as well as helping to identify a bound water molecule in Bacillus PS3 whose presence was previously overlooked due to the limited resolution of the structural data.

Cooperation among c-subunits of FoF1-ATP synthase in rotation-coupled proton translocation

Simulations revealed that prolonged proton uptake in mutated c-subunits is shared between two c- subunits, explaining the cooperation observed in biochemical assays.

ATP synthase in rotation- coupled proton translocation

In FoF1ATP synthase, proton translocation through Fo drives rotation of the csubunit oligomeric ring relative to the asubunit. Recent studies suggest that in each step of the rotation, key glutamic

References

SHOWING 1-10 OF 28 REFERENCES

Aqueous Access Channels in Subunit a of Rotary ATP Synthase*

This report substituted Cys into a 19-residue span of the fourth TMH of subunit a and used chemical modification to obtain information about the aqueous accessibility of residues along this helix, which revealed N-ethylmaleimide-accessible from the cytoplasmic side of the membrane and may lie on the H+ transport route.

Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane

The role of subunit a in promoting proton translocation and rotary motion in the Escherichia coli F1Fo ATP synthase is poorly understood and substitution into the second and fifth TMHs of sub unit a and chemical modification with Ag+ and N-ethylmaleimide are carried out to define the aqueous accessibility of residues along these helices.

Aqueous Access Pathways in ATP Synthase Subunit a

It is concluded that aqueous access from the periplasmic side of F0 to cAsp-61 at the center of the membrane is likely to be mediated by residues of TMHs 2, 3, 4, and 5 at the centers of a four-helix bundle.

The Cytoplasmic Loops of Subunit a of Escherichia coli ATP Synthase May Participate in the Proton Translocating Mechanism*

It is suggested that the Ag+-sensitive domain may be involved in gating H+ release at the cytoplasmic side of the aqueous access channel extending through F0.

Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase.

The shape and charge distribution of the molecular surface of the monomericprotein suggest a packing arrangement for the oligomeric protein in the F0 complex, with the front face of one monomer packing favorably against the back face of a second monomer.

Mode of interaction of the single a subunit with the multimeric c subunits during the translocation of the coupling ions by F1F0 ATPases

An ion translocation mechanism through F0 that in the ATP hydrolysis mode involves binding of the coupling ions from the cytoplasm to the multiple c subunits, ATP‐driven rotation to bring a Na+, Li+, or H+‐loaded c subunit into a contact site with the a subunit and release of the coupled ions through the aSubunit channel to the periplasmic surface of the membrane.

Scanning Cysteine Accessibility of EmrE, an H+-coupled Multidrug Transporter from Escherichia coli, Reveals a Hydrophobic Pathway for Solutes*

EmrE is a 12-kDa Escherichia colimultidrug transporter that confers resistance to a wide variety of toxic reagents by actively removing them in exchange for hydrogen ions but the substrates are translocated through a hydrophobic pathway.

Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase

The results provide unique new insights into the structure and function of rotary ATP synthases and explain how ATP production is coupled to proton translocation.

Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase.

It is shown that the ring of c subunits in the F(o) part moves along with the gamma and epsilon subunits, and unequivocally place the c subunit oligomer in the rotor part of this molecular machine.