2bl2
THE MEMBRANE ROTOR OF THE V-TYPE ATPASE FROM ENTEROCOCCUS HIRAE
OverviewOverview
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.
About this StructureAbout this Structure
2BL2 is a Single protein structure of sequence from Enterococcus hirae. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 20:26:22 2008