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TitleStructural and mechanistic insights into the bacterial amyloid secretion channel CsgG.
Journal, issue, pagesNature, Vol. 516, Issue 7530, Page 250-253, Year 2014
Publish dateDec 11, 2014
AuthorsParveen Goyal / Petya V Krasteva / Nani Van Gerven / Francesca Gubellini / Imke Van den Broeck / Anastassia Troupiotis-Tsaïlaki / Wim Jonckheere / Gérard Péhau-Arnaudet / Jerome S Pinkner / Matthew R Chapman / Scott J Hultgren / Stefan Howorka / Rémi Fronzes / Han Remaut /
PubMed AbstractCurli are functional amyloid fibres that constitute the major protein component of the extracellular matrix in pellicle biofilms formed by Bacteroidetes and Proteobacteria (predominantly of the α ...Curli are functional amyloid fibres that constitute the major protein component of the extracellular matrix in pellicle biofilms formed by Bacteroidetes and Proteobacteria (predominantly of the α and γ classes). They provide a fitness advantage in pathogenic strains and induce a strong pro-inflammatory response during bacteraemia. Curli formation requires a dedicated protein secretion machinery comprising the outer membrane lipoprotein CsgG and two soluble accessory proteins, CsgE and CsgF. Here we report the X-ray structure of Escherichia coli CsgG in a non-lipidated, soluble form as well as in its native membrane-extracted conformation. CsgG forms an oligomeric transport complex composed of nine anticodon-binding-domain-like units that give rise to a 36-stranded β-barrel that traverses the bilayer and is connected to a cage-like vestibule in the periplasm. The transmembrane and periplasmic domains are separated by a 0.9-nm channel constriction composed of three stacked concentric phenylalanine, asparagine and tyrosine rings that may guide the extended polypeptide substrate through the secretion pore. The specificity factor CsgE forms a nonameric adaptor that binds and closes off the periplasmic face of the secretion channel, creating a 24,000 Å(3) pre-constriction chamber. Our structural, functional and electrophysiological analyses imply that CsgG is an ungated, non-selective protein secretion channel that is expected to employ a diffusion-based, entropy-driven transport mechanism.
External linksNature / PubMed:25219853 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.8 - 24.0 Å
Structure data

EMDB-2750:
Structure of the CsgG-CsgE complex
Method: EM (single particle) / Resolution: 24.0 Å

PDB-4uv2:
Structure of the curli transport lipoprotein CsgG in a non-lipidated, pre-pore conformation
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-4uv3:
Structure of the curli transport lipoprotein CsgG in its membrane- bound conformation
Method: X-RAY DIFFRACTION / Resolution: 3.59 Å

Source
  • Escherichia coli K-12 (bacteria)
  • escherichia coli str. k-12 substr. mc4100 (bacteria)
KeywordsTRANSPORT PROTEIN / OUTER MEMBRANE PROTEIN / CSGG / CURLI TRANSPORTER / OUTER MEMBRANE LIPOPROTEIN / AMYLOID

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