Journal Article

PreJuSER-111908

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-terminal Type IV Pilin Helices

Yu, X. ; Goforth, C. ; Meyer, C. ; Rachel, R. ; Wirth, R. ; Schröder, G. F.FZJ* ; Egelman, E. H.

2012
Elsevier Amsterdam [u.a.]

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Please use a persistent id in citations: doi:10.1016/j.jmb.2012.05.031

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.

Keyword(s): Archaeal Proteins: chemistry (MeSH) ; Archaeal Proteins: metabolism (MeSH) ; Cryoelectron Microscopy (MeSH) ; Desulfurococcaceae: metabolism (MeSH) ; Fimbriae Proteins: chemistry (MeSH) ; Fimbriae Proteins: metabolism (MeSH) ; Models, Molecular (MeSH) ; Protein Structure, Secondary (MeSH) ; Archaeal Proteins ; Fimbriae Proteins ; J ; electron microscopy (auto) ; helical polymers (auto) ; convergent evolution (auto) ; archaea (auto)

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.).

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)
2. BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung (P45)

Appears in the scientific report 2012

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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