Rapid anisotropic motion of the Ca2+-transport ATPase of the rabbit skeletal muscle sarcoplasmic reticulum.
1H nuclear magnetic resonance techniques were used to study the binding of uridine 5'-triphosphate to the Ca2+-transport ATPase (EC 3.6.1.3) of sarcoplasmic reticulum vesicles from rabbit skeletal muscle. The nuclear spin relaxation times determined for the bound nucleotide are used to characterize the rotational motion of the ATPase to which the nucleotide is bound. The results, assuming an anisotropic model for the motion of the ATPase in the membrane, place a low upper limit on the rotational correlation time of the ATPase. This indicates that the motion of the ATPase in the membrane is quite rapid when compared, for example, with the motion found for other membrane-bound proteins such as rhodopsin.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000266:Adenylyl Imidodiphosphate / Q000494:pharmacology; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D011522:Protons; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D014500:Uracil Nucleotides / Q000378:metabolism*
D011522:Protons; D014500:Uracil Nucleotides; D000266:Adenylyl Imidodiphosphate; D000251:Adenosine Triphosphatases; D002118:Calcium