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 E.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 critical 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.
Merola
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F
Lewit-Bentley
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A
Amler
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E
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005822:Genetic Vectors; D066298:In Vitro Techniques; D051379:Mice; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D011993:Recombinant Fusion Proteins; D000255:Adenosine Triphosphate; D000254:Sodium-Potassium-Exchanging ATPase