Na+ Binding of V-type Na+-ATPase inEnterococcus hirae
نویسندگان
چکیده
منابع مشابه
Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae.
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 helice...
متن کاملThe membrane domain of the Na+-motive V-ATPase from Enterococcus hirae contains a heptameric rotor.
In F-ATPases, ATP hydrolysis is coupled to translocation of ions through membranes by rotation of a ring of c subunits in the membrane. The ring is attached to a central shaft that penetrates the catalytic domain, which has pseudo-3-fold symmetry. The ion translocation pathway lies between the external circumference of the ring and another hydrophobic protein. The H+ or Na+:ATP ratio depends up...
متن کاملSequencing and characterization of the ntp gene cluster for vacuolar-type Na(+)-translocating ATPase of Enterococcus hirae.
We have previously reported the DNA and amino acid sequences for the three genes (ntpA, ntpB, and ntpK) encoding the A, B, and K (proteolipid) subunits, respectively, of Na(+)-translocating ATPase of a eubacterium Enterococcus hirae (Kakinuma, Y., Kakinuma, S., Takase, K., Konishi, K., Igarashi, K., and Yamato, I. (1993) Biochem. Biophys. Res. Commun. 195, 1063-1069). In this paper we report th...
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The dynamically changing protonation states of the six acidic amino acid residues in the ion binding pocket of the Na+, K+ -ATPase (NKA) during the ion transport cycle are proposed to drive ion binding, release and possibly determine Na+ or K+ selectivity. We use molecular dynamics (MD) and density functional theory (DFT) simulations to determine the protonation scheme of the Na+ bound conforma...
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1 A specific and essential role for Na,K-ATPase α3 in neurons co-expressing α1 and α3* Background: Neurons express two Na,K-ATPase isoforms, the ubiquitous α1 and neuron-specific α3. Result: α3 is important for control of membrane potential and is fully responsible for restoration of large [Na + ] i increases. Conclusion: α1 and α3 are required for basal neuronal function, but α3 controls resto...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1074/jbc.275.18.13415