10.5061/DRYAD.FV8H6
Bulieris, Paula V.
Okinawa Institute of Science and Technology
Shaikh, Nausad H.
Okinawa Institute of Science and Technology
Freddolino, Peter L.
University of Michigan-Ann Arbor
Samatey, Fadel A.
Okinawa Institute of Science and Technology
Data from: Structure of FlgK reveals the divergence of the bacterial
hook-filament junction of Campylobacter
Dryad
dataset
2018
Campylobacter jejuni
2018-11-08T00:00:00Z
2018-11-08T00:00:00Z
en
https://doi.org/10.1038/s41598-017-15837-0
21212361 bytes
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CC0 1.0 Universal (CC0 1.0) Public Domain Dedication
Evolution of a nano-machine consisting of multiple parts, each with a
specific function, is a complex process. A change in one part should
eventually result in changes in other parts, if the overall function is to
be conserved. In bacterial flagella, the filament and the hook have
distinct functions and their respective proteins, FliC and FlgE, have
different three-dimensional structures. The filament functions as a
helical propeller and the hook as a flexible universal joint. Two
proteins, FlgK and FlgL, assure a smooth connectivity between the hook and
the filament. Here we show that, in Campylobacter, the 3D structure of
FlgK differs from that of its orthologs in Salmonella and Burkholderia,
whose structures have previously been solved. Docking the model of the
FlgK junction onto the structure of the Campylobacter hook provides some
clues about its divergence. These data suggest how evolutionary pressure
to adapt to structural constraints, due to the structure of Campylobacter
hook, causes divergence of one element of a supra-molecular complex in
order to maintain the function of the entire flagellar assembly.
flgK_ring_finalStructural model of the complete FlgKcj
ringmixed_ring_finalStructural model of the interface of the FlgKcj ring
and FlgEcj ring