The isolated H4-H5 cytoplasmic loop of Na,K-ATPase overexpressed in Escherichia coli retains its ability to bind ATP.
The H4-H5 loop of the alpha-subunit of mouse brain Na,K-ATPase was expressed and isolated from Escherichia coli cells. Using fluorescence analogues of ATP, this loop was shown to retain its capability to bind ATP. Isolation of a soluble H4-H5 loop with the native ATP binding site is a crucial step for detailed studies of the molecular mechanism of ATP binding and utilisation.
Obsil
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T
Institute of Physiology, Czech Academy of Sciences, Prague, Czech Republic.
Mérola
F
F
Lewit-Bentley
A
A
Amler
E
E
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D001921:Brain; D003593:Cytoplasm / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D004985:Ethenoadenosine Triphosphate / Q000378:metabolism; D005822:Genetic Vectors / Q000138:chemical synthesis; D051379:Mice; D010446:Peptide Fragments / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D011485:Protein Binding / Q000235:genetics; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism*; D000254:Sodium-Potassium-Exchanging ATPase / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism*
D004985:Ethenoadenosine Triphosphate; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D000255:Adenosine Triphosphate; D000254:Sodium-Potassium-Exchanging ATPase