F1-ATPase: A rotary motor made of a single molecule

Article Abstract:

A review was done to describe a single molecule of F1-adenosine triphosphatase (F1-ATPase), a portion of ATP synthase which functions as a rotary motor enzyme. It involves a central rotor which rotates over unlimited angles against a surrounding stator cylinder of a hexamer. ATP synthase consists of a membrane-embedded, proton-conducting portion F0, and a protruding portion F1. Studies on proton flow through F1 showed that ATP synthase comprises an ATP-driven and a proton-driven motor. A comparison of nucleotide-driven molecular motors is discussed.

Analysis, Enzymes, Adenosine triphosphatase, Enzyme structure-activity relationships

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Atomic structure of scallop myosin subfragment S1 complexed with mgADP: a novel conformation of the myosin head

Article Abstract:

A study was conducted to characterize the atomic structure of the scallop myosin subfragment of S1, which is complexed with magnesium adenosine diphosphate. Results revealed that the SH1 helix is unwound in this myosin state and that the converter is differently positioned during this state that causes an unusual orientation of the lever arm that is located near the axis of the actin helix.

Physiological aspects, Scallops, Muscle proteins, Adenosine diphosphate, Myosin, Magnesium in the body, Magnesium (Nutrient)

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