Structural highlights
Function
[NTPK_ENTHA] Involved in ATP-driven sodium extrusion.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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. This site is probably connected to the membrane surface by two half-channels in subunit NtpI, 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.
Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae.,Murata T, Yamato I, Kakinuma Y, Leslie AG, Walker JE Science. 2005 Apr 29;308(5722):654-9. Epub 2005 Mar 31. PMID:15802565[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Murata T, Yamato I, Kakinuma Y, Leslie AG, Walker JE. Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae. Science. 2005 Apr 29;308(5722):654-9. Epub 2005 Mar 31. PMID:15802565
