The structure of the V-1-ATPase determined by three-dimensional electron microscopy of single particles

Citation
M. Radermacher et al., The structure of the V-1-ATPase determined by three-dimensional electron microscopy of single particles, J STRUCT B, 135(1), 2001, pp. 26-37
Citations number
35
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF STRUCTURAL BIOLOGY
ISSN journal
10478477 → ACNP
Volume
135
Issue
1
Year of publication
2001
Pages
26 - 37
Database
ISI
SICI code
1047-8477(200107)135:1<26:TSOTVD>2.0.ZU;2-U
Abstract
We determined the structure of the V-1-ATPase from Manduca sexta to a resol ution 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 s talk 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 le ngth of the A(3)B(3) hexamer. Inside the cavity the central stalk can be se en connected to only two of the catalytic A subunits. The structure was obt ained by a combination of the Random Conical Reconstruction Technique and a ngular 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, a nd the Two-Step Radon Inversion Algorithm. (C) 2001 Academic Press.