Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG
| Autor: | Jerome S. Pinkner, Rémi Fronzes, Francesca Gubellini, Parveen Goyal, Petya V. Krasteva, Han Remaut, Imke Van den Broeck, Gérard Pehau-Arnaudet, Matthew George Chapman, Scott J. Hultgren, Anastassia Troupiotis-Tsaïlaki, Wim Jonckheere, Nani Van Gerven, Stefan Howorka |
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| Přispěvatelé: | VIB-VUB Center for Structural Biology [Bruxelles], VIB [Belgium], Vrije Universiteit Brussel (VUB), Biologie Structurale de la Sécrétion Bactérienne, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Université libre de Bruxelles (ULB), Washington University School of Medicine in St. Louis, Washington University in Saint Louis (WUSTL), University of Michigan [Ann Arbor], University of Michigan System, University College of London [London] (UCL), This research was supported by VIB through project grant PRJ9 (P.G., N.V.G. and H.R.), by Hercules Foundation through equipment grant UABR/09/005, by National Institutes of Health RO1 grants AI099099 and AI048689 (J.P. and S.J.H.) and A1073847 (M.R.C.), and by Institut Pasteur and Centre national de la recherche scientifique (F.G., G.P.A. and R.F.). S.H. is funded by the Engineering and Physical Sciences Research Council (Institutional Sponsorship Award), the National Physical Laboratory and University College London Chemistry. F.G. is the recipient of a ‘Bourse Roux’ from Institut Pasteur. P.V.K. was supported by the European Research Council (ERC)., Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Faculty of Sciences and Bioengineering Sciences, Structural Biology Brussels, Department of Bio-engineering Sciences |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Protein Conformation Entropy transmembrane signalling MESH: Escherichia coli Proteins 02 engineering and technology curli Crystallography X-Ray MESH: Membrane Transport Proteins Cell membrane Diffusion Protein structure MESH: Protein Conformation HasR Serratia marcescens 0303 health sciences Multidisciplinary [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Membrane transport protein MESH: Escherichia coli Escherichia coli Proteins MESH: Periplasm MESH: Diffusion 021001 nanoscience & nanotechnology MESH: Lipoproteins MESH: Entropy Transmembrane protein Transport protein Protein Transport medicine.anatomical_structure Biochemistry Periplasm 0210 nano-technology Bacterial outer membrane MESH: Models Molecular Amyloid MESH: Protein Transport Lipoproteins [PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph] MESH: Biofilms [SDV.BC]Life Sciences [q-bio]/Cellular Biology Biology Models Biological Article 03 medical and health sciences bacterial nutrient transporter medicine Escherichia coli [CHIM.CRIS]Chemical Sciences/Cristallography Secretion [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology 030304 developmental biology MESH: Amyloid Cell Membrane MESH: Models Biological Membrane Transport Proteins haem Periplasmic space MESH: Crystallography X-Ray Biofilms Biophysics biology.protein [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM] integrative approach MESH: Cell Membrane |
| Zdroj: | Nature Nature, 2014, 516 (7530), pp.250-253. ⟨10.1038/nature13768⟩ Nature, Nature Publishing Group, 2014, 516 (7530), pp.250-253. ⟨10.1038/nature13768⟩ |
| ISSN: | 0028-0836 1476-4687 1476-4679 |
| DOI: | 10.1038/nature13768⟩ |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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