4XE5

Crystal structure of the Na,K-ATPase from bovine

Summary for 4XE5

• Entry DOI: 10.2210/pdb4xe5/pdb
• Descriptor: Sodium/potassium-transporting ATPase subunit alpha-1, Sodium/potassium-transporting ATPase subunit beta, Sodium/potassium-transporting ATPase subunit gamma, ... (7 entities in total)
• Functional Keywords: alpha-helical transmembrane protein, atpase, sodium ion transport, potassium ion transport, atp binding, sodium binding, receptor for cardiotonic steroids, plasma membrane, hydrolase, membrane protein, multisubunit complex, beryllium trifluoride
• Biological source: Bos taurus (Bovine); More
• Cellular location: Cell membrane, sarcolemma ; Multi-pass membrane protein : Q08DA1; Membrane : G3MWR4; Membrane ; Single-pass type III membrane protein : Q04645
• Total number of polymer chains: 3
• Total formula weight: 155876.24

Authors

Gregersen, J.L.,Mattle, D.,Fedosova, N.U.,Nissen, P.,Reinhard, L. (deposition date: 2014-12-22, release date: 2016-03-09, Last modification date: 2024-11-06)

Primary citation

Gregersen, J.L.,Mattle, D.,Fedosova, N.U.,Nissen, P.,Reinhard, L.
Isolation, crystallization and crystal structure determination of bovine kidney Na(+),K(+)-ATPase.
Acta Crystallogr.,Sect.F, 72:282-287, 2016

PubMed Abstract: 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 Å with full completeness to a resolution of 4.2 Å. The structure was determined by molecular replacement, revealing unbiased electron-density features for bound BeF3(-), ouabain and Mg(2+) ions.

PubMed: 27050261
DOI: 10.1107/S2053230X1600279X

Experimental method

X-RAY DIFFRACTION (3.901 Å)