2bl2 | pdb_00002bl2

THE MEMBRANE ROTOR OF THE V-TYPE ATPASE FROM ENTEROCOCCUS HIRAE

spinqualitylabelsall models 2bl2, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bl2 is a 10 chain structure with sequence from Enterococcus hirae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: LHG, NA, UMQ Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Resources: FirstGlance, OCA, RCSB, PDBsum Function [NTPK_ENTHR] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase V-ATPase

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