We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy.
- Authors
Yonekura, Koji; Maki-Yonekura, Saori; Namba, Keiichi
- Abstract
The bacterial flagellar filament is a helical propeller for bacterial locomotion. It is a helical assembly of a single protein, flagellin, and its tubular structure is formed by 11 protofilaments in two distinct conformations, L- and R-type, for supercoiling. The X-ray crystal structure of a flagellin fragment lacking about 100 terminal residues revealed the protofilament structure, but the full filament structure is still essential for understanding the mechanism of supercoiling and polymerization. Here we report a complete atomic model of the R-type filament by electron cryomicroscopy. A density map obtained from image data up to 4 A resolution shows the feature of alpha-helical backbone and some large side chains. The atomic model built on the map reveals intricate molecular packing and an alpha-helical coiled coil formed by the terminal chains in the inner core of the filament, with its intersubunit hydrophobic interactions having an important role in stabilizing the filament.
- Publication
Nature, 2003, Vol 424, Issue 6949, p643
- ISSN
1476-4687
- Publication type
Journal Article
- DOI
10.1038/nature01830