Filaments from Ignicoccus hospitalis show diversity of packing in proteins containing N-terminal type IV pilin helices.
Bacterial motility is driven by the rotation of flagellar filaments that supercoil. The supercoiling involves the switching of coiled-coil protofilaments between two different states. In archaea, the flagellar filaments responsible for motility are formed by proteins with distinct homology in their N-terminal portion to bacterial Type IV pilins. The bacterial pilins have a single N-terminal hydrophobic α-helix, not the coiled coil found in flagellin. We have used electron cryo-microscopy to study the adhesion filaments from the archaeon Ignicoccus hospitalis. While I. hospitalis is non-motile, these filaments make transitions between rigid stretches and curved regions and appear morphologically similar to true archaeal flagellar filaments. A resolution of ~7.5Å allows us to unambiguously build a model for the packing of these N-terminal α-helices, and this packing is different from several bacterial Type IV pili whose structure has been analyzed by electron microscopy and modeling. Our results show that the mechanism responsible for the supercoiling of bacterial flagellar filaments cannot apply to archaeal filaments.
Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908-0733, USA.
Xiong
X
Yu
Charles
C
Goforth
Carolin
C
Meyer
Reinhard
R
Rachel
Reinhard
R
Wirth
Gunnar F
GF
Schröder
Edward H
EH
Egelman
D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D020285:Cryoelectron Microscopy; D019620:Desulfurococcaceae / Q000378:metabolism*; D036781:Fimbriae Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D017433:Protein Structure, Secondary
D019843:Archaeal Proteins; D036781:Fimbriae Proteins