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@ARTICLE{Yu:111908,
      author       = {Yu, X. and Goforth, C. and Meyer, C. and Rachel, R. and
                      Wirth, R. and Schröder, G.F. and Egelman, E.H.},
      title        = {{F}ilaments from {I}gnicoccus hospitalis {S}how {D}iversity
                      of {P}acking in {P}roteins {C}ontaining {N}-terminal {T}ype
                      {IV} {P}ilin {H}elices},
      journal      = {Journal of molecular biology},
      volume       = {422},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-111908},
      pages        = {274 - 281},
      year         = {2012},
      note         = {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.).},
      abstract     = {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.},
      keywords     = {Archaeal Proteins: chemistry / Archaeal Proteins:
                      metabolism / Cryoelectron Microscopy / Desulfurococcaceae:
                      metabolism / Fimbriae Proteins: chemistry / Fimbriae
                      Proteins: metabolism / Models, Molecular / Protein
                      Structure, Secondary / Archaeal Proteins (NLM Chemicals) /
                      Fimbriae Proteins (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22659006},
      UT           = {WOS:000308681000010},
      doi          = {10.1016/j.jmb.2012.05.031},
      url          = {https://juser.fz-juelich.de/record/111908},
}