Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

The Structure of the V1-ATPase Determined by Three-Dimensional Electron Microscopy of Single Particles

MPG-Autoren
/persons/resource/persons137844

Radermacher,  Michael
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137863

Ruiz,  Teresa
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Radermacher, M., Ruiz, T., Wieczorek, H., & Grüber, G. (2001). The Structure of the V1-ATPase Determined by Three-Dimensional Electron Microscopy of Single Particles. Journal of Structural Biology, 135(1), 26-37. doi:10.1006/jsbi.2001.4395.


Zitierlink: https://hdl.handle.net/21.11116/0000-0007-3332-7
Zusammenfassung
We determined the structure of the V1-ATPase from Manduca sexta to a resolution of 1.8 nm, which for the first time reveals internal features of the enzyme. The V1-ATPase consists of a headpiece of 13.5 nm in diameter, with six elongated subunits, A3 and B3, of approximately equal size, and a stalk of 6 nm in length that connects V1 with the membrane-bound domain, V0. At the center of the molecule is a cavity that extends throughout the length of the A3B3 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° images, contrast transfer function correction for tilt images, and the Two-Step Radon Inversion Algorithm.