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TitleGastric proton pump with two occluded K engineered with sodium pump-mimetic mutations.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 5709, Year 2021
Publish dateSep 29, 2021
AuthorsKazuhiro Abe / Kenta Yamamoto / Katsumasa Irie / Tomohiro Nishizawa / Atsunori Oshima /
PubMed AbstractThe gastric H,K-ATPase mediates electroneutral exchange of 1H/1K per ATP hydrolysed across the membrane. Previous structural analysis of the K-occluded E2-P transition state of H,K-ATPase showed a ...The gastric H,K-ATPase mediates electroneutral exchange of 1H/1K per ATP hydrolysed across the membrane. Previous structural analysis of the K-occluded E2-P transition state of H,K-ATPase showed a single bound K at cation-binding site II, in marked contrast to the two K ions occluded at sites I and II of the closely-related Na,K-ATPase which mediates electrogenic 3Na/2K translocation across the membrane. The molecular basis of the different K stoichiometry between these K-counter-transporting pumps is elusive. We show a series of crystal structures and a cryo-EM structure of H,K-ATPase mutants with changes in the vicinity of site I, based on the structure of the sodium pump. Our step-wise and tailored construction of the mutants finally gave a two-K bound H,K-ATPase, achieved by five mutations, including amino acids directly coordinating K (Lys791Ser, Glu820Asp), indirectly contributing to cation-binding site formation (Tyr340Asn, Glu936Val), and allosterically stabilizing K-occluded conformation (Tyr799Trp). This quintuple mutant in the K-occluded E2-P state unambiguously shows two separate densities at the cation-binding site in its 2.6 Å resolution cryo-EM structure. These results offer new insights into how two closely-related cation pumps specify the number of K accommodated at their cation-binding site.
External linksNat Commun / PubMed:34588453 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.6 - 3.4 Å
Structure data

31294

7et1

EMDB-31294, PDB-7et1:
Cryo-EM structure of the gastric proton pump K791S/E820D/Y340N/E936V/Y799W mutant in K+-occluded (K+)E2-AlF state
Method: EM (single particle) / Resolution: 2.6 Å

PDB-7efl:
Crystal structure of the gastric proton pump K791S in (BYK)E2BeF state
Method: X-RAY DIFFRACTION / Resolution: 3.4 Å

PDB-7efm:
Crystal structure of the gastric proton pump K791S/E820D/Y340N in (BYK)E2BeF state
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-7efn:
Crystal structure of the gastric proton pump K791S/E820D/Y340N/E936V in (BYK)E2BeF state
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-RB:
RUBIDIUM ION

ChemComp-J3C:
(7R,8R,9S)-2,3-dimethyl-9-phenyl-7,8,9,10-tetrahydroimidazo[1,2-h][1,7]naphthyridine-7,8-diol

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

ChemComp-PCW:
1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DOPC, phospholipid*YM

ChemComp-K:
Unknown entry

ChemComp-ALF:
TETRAFLUOROALUMINATE ION

ChemComp-CLR:
CHOLESTEROL

Source
  • sus scrofa (pig)
KeywordsMEMBRANE PROTEIN / Cation pump / P-type ATPase / gastric / proton pump / gastric proton pump / primary transporter / transporter

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