Publication Abstract from PubMed
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.
Inter-subunit interaction of gastric H+,K+-ATPase prevents reverse reaction of the transport cycle.,Abe K, Tani K, Nishizawa T, Fujiyoshi Y EMBO J. 2009 Jun 3;28(11):1637-43. Epub 2009 Apr 23. PMID:19387495[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
