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TitleInter-subunit interaction of gastric H+,K+-ATPase prevents reverse reaction of the transport cycle.
Journal, issue, pagesEMBO J, Vol. 28, Issue 11, Page 1637-1643, Year 2009
Publish dateJun 3, 2009
AuthorsKazuhiro Abe / Kazutoshi Tani / Tomohiro Nishizawa / Yoshinori Fujiyoshi /
PubMed AbstractThe gastric H(+),K(+)-ATPase is an ATP-driven proton pump responsible for generating a million-fold proton gradient across the gastric membrane. We present the structure of gastric H(+),K(+)-ATPase ...The gastric H(+),K(+)-ATPase is an ATP-driven proton pump responsible for generating a million-fold proton gradient across the gastric membrane. We present the structure of gastric H(+),K(+)-ATPase at 6.5 A resolution as determined by electron crystallography of two-dimensional crystals. The structure shows the catalytic alpha-subunit and the non-catalytic beta-subunit in a pseudo-E(2)P conformation. Different from Na(+),K(+)-ATPase, the N-terminal tail of the beta-subunit is in direct contact with the phosphorylation domain of the alpha-subunit. This interaction may hold the phosphorylation domain in place, thus stabilizing the enzyme conformation and preventing the reverse reaction of the transport cycle. Indeed, truncation of the beta-subunit N-terminus allowed the reverse reaction to occur. These results suggest that the beta-subunit N-terminus prevents the reverse reaction from E(2)P to E(1)P, which is likely to be relevant for the generation of a large H(+) gradient in vivo situation.
External linksEMBO J / PubMed:19387495 / PubMed Central
MethodsEM (electron crystallography)
Resolution6.5 Å
Structure data

5104

3ixz

EMDB-5104: Gastric H,K-ATPase complexed with aluminum fluoride
PDB-3ixz: Pig gastric H+/K+-ATPase complexed with aluminium fluoride
Method: EM (electron crystallography) / Resolution: 6.5 Å

Source
  • sus scrofa (pig)
KeywordsHYDROLASE / ION PUMP / H+ / K+-ATPASE / P-TYPE ATPASE / MEMBRANE PROTEIN / E2 / ALUMINIUM FLUORIDE / ATP-binding / Hydrogen ion transport / Ion transport / Magnesium / Membrane / Metal-binding / Nucleotide-binding / Phosphoprotein / Potassium / Potassium transport / Transmembrane / Transport / Disulfide bond / Glycoprotein / Signal-anchor

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