- PDB-4uv2: Structure of the curli transport lipoprotein CsgG in a non-lipida... -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 4uv2
Title
Structure of the curli transport lipoprotein CsgG in a non-lipidated, pre-pore conformation
Components
CURLI PRODUCTION TRANSPORT COMPONENT CSGG
Keywords
TRANSPORT PROTEIN / OUTER MEMBRANE PROTEIN
Function / homology
Function and homology information
curli secretion complex / curli assembly / protein secretion by the type VIII secretion system / protein transmembrane transport / single-species biofilm formation / cell outer membrane / outer membrane-bounded periplasmic space / identical protein binding / plasma membrane Similarity search - Function
Curli production assembly/transport component CsgG / Curli production assembly/transport component CsgG / Prokaryotic membrane lipoprotein lipid attachment site profile. Similarity search - Domain/homology
Journal: Nature / Year: 2014 Title: Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG. Authors: Parveen Goyal / Petya V Krasteva / Nani Van Gerven / Francesca Gubellini / Imke Van den Broeck / Anastassia Troupiotis-Tsaïlaki / Wim Jonckheere / Gérard Péhau-Arnaudet / Jerome S Pinkner ...Authors: Parveen 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 / Abstract: 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 ...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.
#262 - Oct 2021 Fifty Years of Open Access to PDB Structures similarity (1)
#29 - May 2002 Penicillin-binding Proteins similarity (1)
#95 - Nov 2007 Multidrug Resistance Transporters similarity (1)
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Assembly
Deposited unit
A: CURLI PRODUCTION TRANSPORT COMPONENT CSGG B: CURLI PRODUCTION TRANSPORT COMPONENT CSGG C: CURLI PRODUCTION TRANSPORT COMPONENT CSGG D: CURLI PRODUCTION TRANSPORT COMPONENT CSGG E: CURLI PRODUCTION TRANSPORT COMPONENT CSGG F: CURLI PRODUCTION TRANSPORT COMPONENT CSGG G: CURLI PRODUCTION TRANSPORT COMPONENT CSGG H: CURLI PRODUCTION TRANSPORT COMPONENT CSGG I: CURLI PRODUCTION TRANSPORT COMPONENT CSGG J: CURLI PRODUCTION TRANSPORT COMPONENT CSGG K: CURLI PRODUCTION TRANSPORT COMPONENT CSGG L: CURLI PRODUCTION TRANSPORT COMPONENT CSGG M: CURLI PRODUCTION TRANSPORT COMPONENT CSGG N: CURLI PRODUCTION TRANSPORT COMPONENT CSGG O: CURLI PRODUCTION TRANSPORT COMPONENT CSGG P: CURLI PRODUCTION TRANSPORT COMPONENT CSGG
A: CURLI PRODUCTION TRANSPORT COMPONENT CSGG B: CURLI PRODUCTION TRANSPORT COMPONENT CSGG C: CURLI PRODUCTION TRANSPORT COMPONENT CSGG D: CURLI PRODUCTION TRANSPORT COMPONENT CSGG E: CURLI PRODUCTION TRANSPORT COMPONENT CSGG F: CURLI PRODUCTION TRANSPORT COMPONENT CSGG G: CURLI PRODUCTION TRANSPORT COMPONENT CSGG H: CURLI PRODUCTION TRANSPORT COMPONENT CSGG
I: CURLI PRODUCTION TRANSPORT COMPONENT CSGG J: CURLI PRODUCTION TRANSPORT COMPONENT CSGG K: CURLI PRODUCTION TRANSPORT COMPONENT CSGG L: CURLI PRODUCTION TRANSPORT COMPONENT CSGG M: CURLI PRODUCTION TRANSPORT COMPONENT CSGG N: CURLI PRODUCTION TRANSPORT COMPONENT CSGG O: CURLI PRODUCTION TRANSPORT COMPONENT CSGG P: CURLI PRODUCTION TRANSPORT COMPONENT CSGG
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.9795 Å / Relative weight: 1
Reflection
Resolution: 2.8→30 Å / Num. obs: 112419 / % possible obs: 98.7 % / Observed criterion σ(I): 2 / Redundancy: 11.2 % / Biso Wilson estimate: 46.8 Å2 / Rmerge(I) obs: 0.15 / Net I/σ(I): 9.82
Reflection shell
Resolution: 2.8→2.9 Å / Redundancy: 7 % / Rmerge(I) obs: 0.81 / Mean I/σ(I) obs: 2 / % possible all: 98.3
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Processing
Software
Name
Version
Classification
PHENIX
(PHENIX.REFINE)
refinement
XDS
datareduction
XSCALE
datascaling
XSCALE
phasing
Refinement
Method to determine structure: SAD Starting model: NONE Resolution: 2.8→29.765 Å / SU ML: 0.35 / σ(F): 2.12 / Phase error: 23.79 / Stereochemistry target values: MLHL Details: DISORDERED SIDECHAINS WERE MODELED STEREOCHEMICALLY AND ARE INDICATED BY A 0 OCCUPANCY
Rfactor
Num. reflection
% reflection
Rfree
0.2337
5620
5 %
Rwork
0.1881
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obs
0.1903
112369
98.98 %
Solvent computation
Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL