|Entry||Database: PDB / ID: 6rbk|
|Title||Cryo-EM structure of the anti-feeding prophage (AFP) baseplate in extended state, 3-fold symmetrised|
|Keywords||VIRUS LIKE PARTICLE / Anti-feeding prophage / secretion system / AFP / contractile / baseplate|
|Function / homology||Vgr protein, OB-fold domain superfamily / Type VI secretion system/phage-baseplate injector OB domain / Afp8 / Afp7|
Function and homology information
|Biological species||Serratia entomophila (bacteria)|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å|
|Citation||Journal: 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.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
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Mass: 25259.434 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Serratia entomophila (bacteria) / Gene: afp7 / Production host: Escherichia coli (E. coli) / References: UniProt: Q6HAD2
Mass: 58091.715 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Serratia entomophila (bacteria) / Gene: afp8 / Production host: Escherichia coli (E. coli) / References: UniProt: Q6HAD1
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Component||Name: Cryo-EM structure of the anti-feeding prophage (AFP) baseplate in extended state, 3-fold symmetrised|
Details: A scaling by a factor of 2 is recommended for visualisation
Entity ID: 1,2 / Source: RECOMBINANT
|Molecular weight||Units: MEGADALTONS / Experimental value: NO|
|Source (natural)||Organism: Serratia entomophila (bacteria)|
|Source (recombinant)||Organism: Escherichia coli (E. coli)|
|Buffer solution||pH: 7|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 20 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Particle selection||Num. of particles selected: 46991|
|Symmetry||Point symmetry: C6 (6 fold cyclic)|
|3D reconstruction||Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 46991 / Symmetry type: POINT|
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