期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 72, 期 -, 页码 282-287出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X1600279X
关键词
P-type ATPase; native source isolation; cardiotonic steroids; Na+, K+-ATPase; ouabain
资金
- Danish Council for Independent Research
- Graduate School of Science and Technology, Aarhus University
- European Research Council through the Advanced Research Grant BIOMEMOS
- Danish Council for Independent Research - Medical Science
- Novo Nordisk Fonden [NNF12OC0002082] Funding Source: researchfish
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 C222(1) with one molecule in the asymmetric unit exhibited anisotropic diffraction to a resolution of 3.7 angstrom with full completeness to a resolution of 4.2 angstrom. The structure was determined by molecular replacement, revealing unbiased electron-density features for bound BeF3-, ouabain and Mg2+ ions.
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