Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae.

  title={Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae.},
  author={Takeshi Murata and Ichiro Yamato and Yoshimi Kakinuma and Andrew G. W. Leslie and John E Walker},
  volume={308 5722},
The membrane rotor ring from the vacuolar-type (V-type) sodium ion-pumping adenosine triphosphatase (Na+-ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which are homologs of the 16-kilodalton and 8-kilodalton proteolipids found in other V-ATPases and in F1Fo- or F-ATPases, respectively. Each NtpK subunit has four transmembrane alpha helices, with a sodium ion bound between helices 2 and 4 at a site buried deeply in the membrane that includes the essential residue glutamate-139… CONTINUE READING
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