Journal
SCIENCE
Volume 308, Issue 5722, Pages 654-659Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1110064
Keywords
-
Categories
Ask authors/readers for more resources
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 proteotipids found in other V-ATPases and in F1F0- or F-ATPases, respectively. Each NtpK subunit has four transmembrane a 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. This site is probably connected to the membrane surface by two half-channels in subunit Ntpl, against which the ring rotates. Symmetry mismatch between the rotor and catalytic domains appears to be an intrinsic feature of both V- and F-ATPases.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available