The structure of the V(1)-ATPase determined by three-dimensional electron microscopy of single particles |
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Authors: | Radermacher M Ruiz T Wieczorek H Grüber G |
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Institution: | Max-Planck-Institut für Biophysik, Abt. Strukturbiologie, Heinrich Hoffmann Strasse 7, Frankfurt/M., D-60528, Germany. michael.radermacher@mpibp-frankfurt.mpg.de |
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Abstract: | We determined the structure of the V(1)-ATPase from Manduca sexta to a resolution of 1.8 nm, which for the first time reveals internal features of the enzyme. The V(1)-ATPase consists of a headpiece of 13.5 nm in diameter, with six elongated subunits, A(3) and B(3), of approximately equal size, and a stalk of 6 nm in length that connects V(1) with the membrane-bound domain, V(O). At the center of the molecule is a cavity that extends throughout the length of the A(3)B(3) hexamer. Inside the cavity the central stalk can be seen connected to only two of the catalytic A subunits. The structure was obtained by a combination of the Random Conical Reconstruction Technique and angular refinements. Additional recently developed techniques that were used include methods for simultaneous translational rotational alignment of the 0 degrees images, contrast transfer function correction for tilt images, and the Two-Step Radon Inversion Algorithm. |
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