2XZB

Pig Gastric H,K-ATPase with bound BeF and SCH28080

Summary for 2XZB

• Entry DOI: 10.2210/pdb2xzb/pdb
• Related: 1IWC 1IWF 3A3Y
• EMDB information: 1831
• Descriptor: POTASSIUM-TRANSPORTING ATPASE ALPHA CHAIN 1, POTASSIUM-TRANSPORTING ATPASE SUBUNIT BETA (2 entities in total)
• Functional Keywords: hydrolase, ion pump, h/k-atpase, p-type atpase, membrane protein, beryllium fluoride, atp-binding, acid suppressant
• Biological source: SUS SCROFA (PIG); More
• Total number of polymer chains: 2
• Total formula weight: 147513.53

Authors

Abe, K.,Tani, K.,Fujiyoshi, Y. (deposition date: 2010-11-24, release date: 2011-01-26, Last modification date: 2020-09-16)

Primary citation

Abe, K.,Tani, K.,Fujiyoshi, Y.
Conformational Rearrangement of Gastric H(+),K(+)- ATPase Induced by an Acid Suppressant.
Nat.Commun., 2:155-, 2011

PubMed Abstract: 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.

PubMed: 21224846
DOI: 10.1038/NCOMMS1154

Experimental method

ELECTRON CRYSTALLOGRAPHY (7 Å)