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TitleConformational rearrangement of gastric H(+),K(+)-ATPase induced by an acid suppressant.
Journal, issue, pagesNat Commun, Vol. 2, Page 155, Year 2011
Publish dateJan 11, 2011
AuthorsKazuhiro Abe / Kazutoshi Tani / Yoshinori Fujiyoshi /
PubMed AbstractAcid-related gastric diseases are associated with disorder of digestive tract acidification. The gastric proton pump, H(+),K(+)-ATPase, exports H(+) in exchange for luminal K(+) to generate a highly ...Acid-related gastric diseases are associated with disorder of digestive tract acidification. The gastric proton pump, H(+),K(+)-ATPase, exports H(+) in exchange for luminal K(+) to generate a highly acidic environment in the stomach, and is a main target for acid suppressants. Here, we report the three-dimensional structure of gastric H(+),K(+)-ATPase with bound SCH28080, a representative K(+)-competitive acid blocker, at 7 Å resolution based on electron crystallography of two-dimensional crystals. The density of the bound SCH28080 is found near transmembrane (TM) helices 4, 5 and 6, in the luminal cavity. The SCH28080-binding site is formed by the rearrangement of TM helices, which is in turn transmitted to the cytoplasmic domains, resulting in a luminal-open conformation. These results represent the first structural evidence for a binding site of an acid suppressant on H(+),K(+)-ATPase, and the conformational change induced by this class of drugs.
External linksNat Commun / PubMed:21224846 / PubMed Central
MethodsEM (electron crystallography)
Resolution7.0 Å
Structure data

1831

2xzb

EMDB-1831, PDB-2xzb:
Pig Gastric H,K-ATPase with bound BeF and SCH28080
Method: EM (electron crystallography) / Resolution: 7.0 Å

Source
  • sus scrofa (pig)
KeywordsHYDROLASE / ION PUMP / H/K-ATPASE / P-TYPE ATPASE / MEMBRANE PROTEIN / BERYLLIUM FLUORIDE / ATP-BINDING / ACID SUPPRESSANT

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