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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-0947 | |||||||||
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Title | Low resolution architecture of curli complex | |||||||||
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![]() | curli / TRANSPORT PROTEIN | |||||||||
Function / homology | ![]() 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 | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.24 Å | |||||||||
![]() | Zhang M / Shi H | |||||||||
![]() | ![]() Title: Cryo-EM structure of the nonameric CsgG-CsgF complex and its implications for controlling curli biogenesis in Enterobacteriaceae. Authors: Manfeng Zhang / Huigang Shi / Xuemei Zhang / Xinzheng Zhang / Yihua Huang / ![]() Abstract: Curli play critical roles in biofilm formation, host cell adhesion, and colonization of inert surfaces in many Enterobacteriaceae. In Escherichia coli, curli biogenesis requires 7 curli-specific gene ...Curli play critical roles in biofilm formation, host cell adhesion, and colonization of inert surfaces in many Enterobacteriaceae. In Escherichia coli, curli biogenesis requires 7 curli-specific gene (csg) products-CsgA through G-working in concert. Of them, CsgG and CsgF are 2 outer membrane (OM)-localized components that consists of the core apparatus for secretion and assembly of curli structural subunits, CsgB and CsgA. Here, we report the cryogenic electron microscopy (cryo-EM) structure of CsgG in complex with CsgF from E. coli. The structure reveals that CsgF forms a stable complex with CsgG via a 1:1 stoichiometry by lining the upper lumen of the nonameric CsgG channel via its N-terminal 27 residues, forming a funnel-like entity plugged in the CsgG channel and creating a unique secretion channel with 2 constriction regions, consistent with the recently reported structure of the CsgG-CsgF complex. Functional studies indicate that export of CsgF to the cell surface requires the CsgG channel, and CsgF not only functions as an adaptor that bridges CsgB with CsgG but also may play important roles in controlling the rates of translocation and/or polymerization for curli structural subunits. Importantly, we found that a series of CsgF-derived peptides are able to efficiently inhibit curli production to E. coli when administrated exogenously, highlighting a potential strategy to interfere biofilm formation in E. coli strains. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 59.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.7 KB 17.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.1 KB | Display | ![]() |
Images | ![]() | 51 KB | ||
Filedesc metadata | ![]() | 5.6 KB | ||
Others | ![]() ![]() | 49.5 MB 49.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6lqjMC ![]() 0945C ![]() 6lqhC ![]() 7brmC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: #2
File | emd_0947_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_0947_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : curli core complex of CsgG and CsgF
Entire | Name: curli core complex of CsgG and CsgF |
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Components |
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-Supramolecule #1: curli core complex of CsgG and CsgF
Supramolecule | Name: curli core complex of CsgG and CsgF / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Curli production assembly/transport component CsgG
Macromolecule | Name: Curli production assembly/transport component CsgG / type: protein_or_peptide / ID: 1 / Number of copies: 9 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 31.62618 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MQRLFLLVAV MLLSGCLTAP PKEAARPTLM PRAQSYKDLT HLPAPTGKIF VSVYNIQDET GQFKPYPASN FSTAVPQSAT AMLVTALKD SRWFIPLERQ GLQNLLNERK IIRAAQENGT VAINNRIPLQ SLTAANIMVE GSIIGYESNV KSGGVGARYF G IGADTQYQ ...String: MQRLFLLVAV MLLSGCLTAP PKEAARPTLM PRAQSYKDLT HLPAPTGKIF VSVYNIQDET GQFKPYPASN FSTAVPQSAT AMLVTALKD SRWFIPLERQ GLQNLLNERK IIRAAQENGT VAINNRIPLQ SLTAANIMVE GSIIGYESNV KSGGVGARYF G IGADTQYQ LDQIAVNLRV VNVSTGEILS SVNTSKTILS YEVQAGVFRF IDYQRLLEGE VGYTSNEPVM LCLMSAIETG VI FLINDGI DRGLWDLQNK AERQNDILVK YRHMSVPPES WSHPQFEK UniProtKB: Curli production assembly/transport component CsgG |
-Macromolecule #2: Curli production assembly/transport component CsgF
Macromolecule | Name: Curli production assembly/transport component CsgF / type: protein_or_peptide / ID: 2 / Number of copies: 9 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 15.894586 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MRVKHAVVLL MLISPLSWAG TMTFQFRNPN FGGNPNNGAF LLNSAQAQNS YKDPSYNDDF GIETPSALDN FTQAIQSQIL GGLLSNINT GKPGRMVTND YIVDIANRDG QLQLNVTDRK TGQTSTIQVS GLQNNSTDFH HHHHH UniProtKB: Curli production assembly/transport component CsgF |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Grid | Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 80 % / Chamber temperature: 298 K |
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Electron microscopy
Microscope | FEI TECNAI ARCTICA |
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Temperature | Min: 70.0 K |
Alignment procedure | Coma free - Residual tilt: 0.1 mrad |
Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K2 BASE (4k x 4k) / Digitization - Dimensions - Width: 3710 pixel / Digitization - Dimensions - Height: 3838 pixel / Number grids imaged: 1 / Number real images: 2500 / Average electron dose: 48.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 70.0 µm / Calibrated defocus max: 2.5 µm / Calibrated defocus min: 1.0 µm / Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |