TY  - JOUR
AU  - Yu, X.
AU  - Goforth, C.
AU  - Meyer, C.
AU  - Rachel, R.
AU  - Wirth, R.
AU  - Schröder, G.F.
AU  - Egelman, E.H.
TI  - Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-terminal Type IV Pilin Helices
JO  - Journal of molecular biology
VL  - 422
SN  - 0022-2836
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - PreJuSER-111908
SP  - 274 - 281
PY  - 2012
N1  - This work was supported by National Institutes of Health grant EB001567 (to E.H.E.) and by WI 731/10-1 from the Deutsche Forschungsgemeinschaft (to R.W. and R.R.).
AB  - 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.
KW  - Archaeal Proteins: chemistry
KW  - Archaeal Proteins: metabolism
KW  - Cryoelectron Microscopy
KW  - Desulfurococcaceae: metabolism
KW  - Fimbriae Proteins: chemistry
KW  - Fimbriae Proteins: metabolism
KW  - Models, Molecular
KW  - Protein Structure, Secondary
KW  - Archaeal Proteins (NLM Chemicals)
KW  - Fimbriae Proteins (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:22659006
UR  - <Go to ISI:>//WOS:000308681000010
DO  - DOI:10.1016/j.jmb.2012.05.031
UR  - https://juser.fz-juelich.de/record/111908
ER  -