2BL2

The membrane rotor of the V-type ATPase from Enterococcus hirae

Summary for 2BL2

• Entry DOI: 10.2210/pdb2bl2/pdb
• Descriptor: V-TYPE SODIUM ATP SYNTHASE SUBUNIT K, 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE, SODIUM ION, ... (5 entities in total)
• Functional Keywords: v-type atpase, k-ring, membrane rotor, sodium transporter, hydrogen ion transport, hydrolase, transmembrane
• Biological source: ENTEROCOCCUS HIRAE
• Cellular location: Cell membrane; Multi-pass membrane protein (Potential): P43457
• Total number of polymer chains: 10
• Total formula weight: 207742.54

Authors

Murata, T.,Yamato, I.,Kakinuma, Y.,Leslie, A.G.W.,Walker, J.E. (deposition date: 2005-02-25, release date: 2005-04-05, Last modification date: 2024-05-08)

Primary citation

Murata, T.,Yamato, I.,Kakinuma, Y.,Leslie, A.G.W.,Walker, J.E.
Structure of the Rotor of the Vacuolar-Type Na- ATPase from Enterococcus Hirae
Science, 308:654-, 2005

PubMed Abstract: 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.

PubMed: 15802565
DOI: 10.1126/SCIENCE.1110064

Experimental method

X-RAY DIFFRACTION (2.1 Å)