4xe5

Crystal structure of the Na,K-ATPase from bovine

spinqualitylabelsall models 4xe5, resolution 3.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xe5 is a 3 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.901Å Ligands: BFD, CLR, MG, OBN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ATNG_BOVIN May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase. Publication Abstract from PubMed Na(+),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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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