|Entry||Database: EMDB / ID: EMD-4859|
|Title||Cryo-EM structure of the anti-feeding prophage (AFP) sheath-tube in contracted state, C6 symmetrized|
|Sample||Cryo-EM structure of the anti-feeding prophage (AFP) baseplate in contracted state|
|Biological species||Serratia entomophila (bacteria)|
|Method||single particle reconstruction / cryo EM / Resolution: 4.2 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.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_4859.map.gz / Format: CCP4 / Size: 184 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.397 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Supplemental map: emd 4859 half map 1.map
|Projections & Slices|
-Supplemental map: emd 4859 half map 2.map
-Entire Cryo-EM structure of the anti-feeding prophage (AFP) baseplate in...
|Entire||Name: Cryo-EM structure of the anti-feeding prophage (AFP) baseplate in contracted state|
Number of components: 1
-Component #1: protein, Cryo-EM structure of the anti-feeding prophage (AFP) bas...
|Protein||Name: Cryo-EM structure of the anti-feeding prophage (AFP) baseplate in contracted state|
Recombinant expression: No
|Source||Species: Serratia entomophila (bacteria)|
|Source (engineered)||Expression System: Escherichia coli (E. coli)|
|Specimen||Specimen state: Filament / Method: cryo EM|
|Sample solution||pH: 7|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 27 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: FEI FALCON II (4k x 4k)|
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