7
August 2003
Flagellin: New view of structure
Crystallization is a necessary first step for most high-resolution studies of the three-dimensional structure of biological macromolecules and their assemblies. But the crystal is often unrepresentative of the functional state of these molecules, so the first report of an atomic model of a protein obtained by electron cryomicroscopy and image analysis alone is a milestone in structural biology. The structure determined is that of the "R-type" bacterial flagellar filament, a helical propeller only 120 – 250 Å in diameter but up to 15 mm in length, and powerful enough to enable bacteria to swim. The new structural map, to 4 Å resolution, reveals an a-helical coiled coil structure at the terminal domains of the flagellin that forms the inner core of the filament, and also how the supercoiled form is affected by subtle changes of amino acid side chains by mutation.
Complete atomic model of the bacterial flagellar filament
by electron cryomicroscopy
KOJI YONEKURA , SAORI
MAKI-YONEKURA & KEIICHI NAMBA
Nature 424, 643–650
(2003); doi:10.1038/nature01830
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