Format

Send to

Choose Destination
See comment in PubMed Commons below
FEBS Lett. 2001 Aug 31;504(3):219-22.

ATP synthase: constrained stoichiometry of the transmembrane rotor.

Author information

1
Max-Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany. daniel.mueller@mpi-cbg.de

Abstract

Recent structural data suggest that the number of identical subunits (c or III) assembled into the cation-powered rotor of F1F0 ATP synthase depends on the biological origin. Atomic force microscopy allowed individual subunits of the cylindrical transmembrane rotors from spinach chloroplast and from Ilyobacter tartaricus ATP synthase to be directly visualized in their native-like environment. Occasionally, individual rotors exhibit structural gaps of the size of one or more subunits. Complete rotors and arch-shaped fragments of incomplete rotors revealed the same diameter within one ATP synthase species. These results suggest the rotor diameter and stoichiometry to be determined by the shape of the subunits and their nearest neighbor interactions.

PMID:
11532457
[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Wiley
    Loading ...
    Support Center