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- W2415671638 abstract "F1-ATPase is a rotary motor enzyme made of a single molecule. The cylinder of F1 has three catalytic sites that mainly locate in β subunits, and two of three sites are fulfilled with nucleotides as directly demonstrated in the single-molecule observation1. Therefore during three stepping of the shaft, 0°→120° →240° →0°, the same nucleotide binds to two different states of β, i.e., β120 and β240, when β0 is denoted as the β in the conformation that waits for ATP-binding.Although the difference of the structural conformation is suggested between β120 and β240 by the direct observation of the orientation of their C-terminal domains under polarization-modulation TIRF microscope2, most structural models have provided identical structures except variations in nucleotide (cf. ref3). To resolve the discrepancy, we here quantified the following parameters of same fluorescent nucleotides in β120 and β240, by the simultaneous observation of the rotation and nucleotide kinetics in F1 under the advanced TIRF microscope. 1) Intensity. 2) Orientation. 3) Linear dichroism in XY-plane. Significant changes were detected in 1 and 3, which indicate the change in microenvironment(s) in the cleft binding a nucleotide. The change possibly correlates with the variation in nucleotide as suggested in models in X-ray crystallography, and may subsequently induce the rotational motions in C-terminal domain of β that trigger the rotation of the shaft.1. T. Nishizaka et al. (2004) Nat. Struct. Mol. Biol.2. T. Masaike, ⋯, Nishizaka, T. (2008) Nat. Struct. Mol. Biol.3. J. P. Abrahams et al. (1994) Nature" @default.
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- W2415671638 date "2016-02-01" @default.
- W2415671638 modified "2023-10-07" @default.
- W2415671638 title "Conformational Change in γ120 and γ240 of F1-ATPase from the Aspect of Difference of Nucleotides by Advanced TIRF Microscope" @default.
- W2415671638 doi "https://doi.org/10.1016/j.bpj.2015.11.915" @default.
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