TY - JOUR
T1 - Conformational change of flagellin for polymorphic supercoiling of the flagellar filament
AU - Maki-Yonekura, Saori
AU - Yonekura, Koji
AU - Namba, Keiichi
N1 - Funding Information:
We thank C.Toyoshima for part of the helical image reconstruction programs, D.A.Agard and J.W.Sedat for support to S.M.-Y.and K.Y.and F.Oosawa,S.Asakura and D.L.D.Caspar for continuous support and encouragement.This work was partly supported by funds from theW.M.KeckAdvanced Microscopy Laboratory at the University of California,San Francisco,to K.Y.and by Grants-in-Aid for Scientific Research (16087207)‘National Project on Protein Structural and FunctionalAnalyses’ from the Ministry of Education,Science and Culture of Japan to K.N.
PY - 2010/4
Y1 - 2010/4
N2 - The bacterial flagellar filament is a helical propeller rotated by the flagellar motor for bacterial locomotion. The filament is a supercoiled assembly of a single protein, flagellin, and is formed by 11 protofilaments. For bacterial taxis, the reversal of motor rotation switches the supercoil between left-and right-handed, both of which arise from combinations of two distinct conformations and packing interactions of the L-type and R-type protofilaments. Here we report an atomic model of the L-type straight filament by electron cryomicroscopy and helical image analysis. Comparison with the R-type structure shows interesting features: an orientation change of the outer core domains (D1) against the inner core domains (D0) showing almost invariant orientation and packing, a conformational switching within domain D1, and the conformational flexibility of domains D0 and D1 with their spoke-like connection for tight molecular packing.
AB - The bacterial flagellar filament is a helical propeller rotated by the flagellar motor for bacterial locomotion. The filament is a supercoiled assembly of a single protein, flagellin, and is formed by 11 protofilaments. For bacterial taxis, the reversal of motor rotation switches the supercoil between left-and right-handed, both of which arise from combinations of two distinct conformations and packing interactions of the L-type and R-type protofilaments. Here we report an atomic model of the L-type straight filament by electron cryomicroscopy and helical image analysis. Comparison with the R-type structure shows interesting features: an orientation change of the outer core domains (D1) against the inner core domains (D0) showing almost invariant orientation and packing, a conformational switching within domain D1, and the conformational flexibility of domains D0 and D1 with their spoke-like connection for tight molecular packing.
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U2 - 10.1038/nsmb.1774
DO - 10.1038/nsmb.1774
M3 - Article
C2 - 20228803
AN - SCOPUS:77950477195
VL - 17
SP - 417
EP - 422
JO - Nature Structural Biology
JF - Nature Structural Biology
SN - 1545-9993
IS - 4
ER -