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- EMDB-4802: Cryo-EM structure of the anti-feeding prophage (AFP) helical shea... -

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Basic information

Entry
Database: EMDB / ID: EMD-4802
TitleCryo-EM structure of the anti-feeding prophage (AFP) helical sheath-tube complex in extended state
Map data
SampleCryo-EM structure of the anti-feeding prophage (AFP) helical sheath-tube complex in extended state:
Afp1 / Afp2 / Afp3
Function / homology
Function and homology information


structural molecule activity
Bacteriophage T4, Gp19, tail tube / Conserved hypothetical protein CHP02241 / Tail sheath protein, C-terminal domain / Tail sheath protein, subtilisin-like domain / Phage tail sheath protein subtilisin-like domain / T4-like virus tail tube protein gp19 / Phage tail sheath C-terminal domain
Afp3 / Afp2 / Afp1
Biological speciesSerratia entomophila (bacteria)
Methodhelical reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsDesfosses A
CitationJournal: Nat Microbiol / Year: 2019
Title: Atomic structures of an entire contractile injection system in both the extended and contracted states.
Authors: Ambroise Desfosses / Hariprasad Venugopal / Tapan Joshi / Jan Felix / Matthew Jessop / Hyengseop Jeong / Jaekyung Hyun / J Bernard Heymann / Mark R H Hurst / Irina Gutsche / Alok K Mitra /
Abstract: Contractile injection systems are sophisticated multiprotein nanomachines that puncture target cell membranes. Although the number of atomic-resolution insights into contractile bacteriophage tails, ...Contractile injection systems are sophisticated multiprotein nanomachines that puncture target cell membranes. Although the number of atomic-resolution insights into contractile bacteriophage tails, bacterial type six secretion systems and R-pyocins is rapidly increasing, structural information on the contraction of bacterial phage-like protein-translocation structures directed towards eukaryotic hosts is scarce. Here, we characterize the antifeeding prophage AFP from Serratia entomophila by cryo-electron microscopy. We present the high-resolution structure of the entire AFP particle in the extended state, trace 11 protein chains de novo from the apical cap to the needle tip, describe localization variants and perform specific structural comparisons with related systems. We analyse inter-subunit interactions and highlight their universal conservation within contractile injection systems while revealing the specificities of AFP. Furthermore, we provide the structure of the AFP sheath-baseplate complex in a contracted state. This study reveals atomic details of interaction networks that accompany and define the contraction mechanism of toxin-delivery tailocins, offering a comprehensive framework for understanding their mode of action and for their possible adaptation as biocontrol agents.
Validation ReportPDB-ID: 6rbn

SummaryFull reportAbout validation report
History
DepositionApr 11, 2019-
Header (metadata) releaseApr 24, 2019-
Map releaseApr 24, 2019-
UpdateAug 14, 2019-
Current statusAug 14, 2019Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.05
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.05
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: : PDB-6rbn
  • Surface level: 0.05
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic models: PDB-6rbn
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

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Map

FileDownload / File: emd_4802.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.35 Å/pix.
x 360 pix.
= 486. Å
1.35 Å/pix.
x 360 pix.
= 486. Å
1.35 Å/pix.
x 360 pix.
= 486. Å

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.35 Å
Density
Contour LevelBy AUTHOR: 0.04 / Movie #1: 0.05
Minimum - Maximum-0.12793036 - 0.2058465
Average (Standard dev.)0.00038390022 (±0.007163424)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-180-180-180
Dimensions360360360
Spacing360360360
CellA=B=C: 486.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.351.351.35
M x/y/z360360360
origin x/y/z0.0000.0000.000
length x/y/z486.000486.000486.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS-180-180-180
NC/NR/NS360360360
D min/max/mean-0.1280.2060.000

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Supplemental data

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Sample components

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Entire Cryo-EM structure of the anti-feeding prophage (AFP) helical shea...

EntireName: Cryo-EM structure of the anti-feeding prophage (AFP) helical sheath-tube complex in extended state
Details: A scaling by a factor of 2 is recommended for visualisation
Number of components: 4

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Component #1: protein, Cryo-EM structure of the anti-feeding prophage (AFP) hel...

ProteinName: Cryo-EM structure of the anti-feeding prophage (AFP) helical sheath-tube complex in extended state
Details: A scaling by a factor of 2 is recommended for visualisation
Recombinant expression: No
SourceSpecies: Serratia entomophila (bacteria)
Source (engineered)Expression System: Escherichia coli (E. coli)

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Component #2: protein, Afp1

ProteinName: Afp1 / Number of Copies: 2 / Recombinant expression: No
MassTheoretical: 16.449449 kDa
SourceSpecies: Serratia entomophila (bacteria)
Source (engineered)Expression System: Escherichia coli (E. coli)

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Component #3: protein, Afp2

ProteinName: Afp2 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 38.784355 kDa
SourceSpecies: Serratia entomophila (bacteria)
Source (engineered)Expression System: Escherichia coli (E. coli)

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Component #4: protein, Afp3

ProteinName: Afp3 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 48.777566 kDa
SourceSpecies: Serratia entomophila (bacteria)
Source (engineered)Expression System: Escherichia coli (E. coli)

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Experimental details

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Sample preparation

SpecimenSpecimen state: Filament / Method: cryo EM
Helical parametersAxial symmetry: C6 (6 fold cyclic) / Delta z: 78.6436 Å / Delta phi: 40.2722 %deg;
Sample solutionpH: 7
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
ImagingMicroscope: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 20 e/Å2 / Illumination mode: FLOOD BEAM
LensImaging mode: BRIGHT FIELD
Specimen HolderModel: OTHER
CameraDetector: GATAN K2 QUANTUM (4k x 4k)

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Image processing

ProcessingMethod: helical reconstruction
3D reconstructionSoftware: RELION / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF
FSC plot (resolution estimation)

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Atomic model buiding

Output model

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