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.
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Article Abstract:
The X-ray crystal structure of the tNS3 NS3 proteinase domain complexed with the NS3-binding region of NS4A is composed of two asymmetric units of tNS3:NS4A molecules. The complex exhibits a three dimensional structure that that adopts a chemotrypsin-like fold with two structural domains that is made of twisted and six-stranded beta sheets. Furthermore, the crystal structure of the complex is similar to the Sinbis virus core protein.
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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.
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