4xe5
From Proteopedia
Crystal structure of the Na,K-ATPase from bovine
Structural highlights
FunctionAT1A1_BOVIN This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (By similarity). Publication Abstract from PubMedNa(+),K(+)-ATPase is responsible for the transport of Na(+) and K(+) across the plasma membrane in animal cells, thereby sustaining vital electrochemical gradients that energize channels and secondary transporters. The crystal structure of Na(+),K(+)-ATPase has previously been elucidated using the enzyme from native sources such as porcine kidney and shark rectal gland. Here, the isolation, crystallization and first structure determination of bovine kidney Na(+),K(+)-ATPase in a high-affinity E2-BeF3(-)-ouabain complex with bound magnesium are described. Crystals belonging to the orthorhombic space group C2221 with one molecule in the asymmetric unit exhibited anisotropic diffraction to a resolution of 3.7 A with full completeness to a resolution of 4.2 A. The structure was determined by molecular replacement, revealing unbiased electron-density features for bound BeF3(-), ouabain and Mg(2+) ions. Isolation, crystallization and crystal structure determination of bovine kidney Na(+),K(+)-ATPase.,Gregersen JL, Mattle D, Fedosova NU, Nissen P, Reinhard L Acta Crystallogr F Struct Biol Commun. 2016 Apr 1;72(Pt 4):282-7. doi:, 10.1107/S2053230X1600279X. Epub 2016 Mar 16. PMID:27050261[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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