YegP-like superfamily / Baseplate protein J-like / Baseplate J-like protein / IraD/Gp25-like / Baseplate wedge protein gp25 / Type VI secretion system, RhsGE-associated Vgr protein / Conserved hypothetical protein CHP02241 / Bacteriophage T4, Gp19, tail tube / T4-like virus tail tube protein gp19 / Gp5/Type VI secretion system Vgr protein, OB-fold domain ...YegP-like superfamily / Baseplate protein J-like / Baseplate J-like protein / IraD/Gp25-like / Baseplate wedge protein gp25 / Type VI secretion system, RhsGE-associated Vgr protein / Conserved hypothetical protein CHP02241 / Bacteriophage T4, Gp19, tail tube / T4-like virus tail tube protein gp19 / Gp5/Type VI secretion system Vgr protein, OB-fold domain / Type VI secretion system/phage-baseplate injector OB domain / Tail sheath protein, subtilisin-like domain / Phage tail sheath protein subtilisin-like domain / Vgr protein, OB-fold domain superfamily / Tail sheath protein, C-terminal domain / Phage tail sheath C-terminal domain Similarity search - Domain/homology
All3325 protein / All3324 protein / All3323 protein / Asl3322 protein / All3321 protein / All3320 protein / All3318 protein / All3317 protein / All3316 protein / All3315 protein / All3314 protein Similarity search - Component
Biological species
Nostoc sp. PCC 7120 = FACHB-418 (bacteria)
Method
single particle reconstruction / cryo EM / Resolution: 2.9 Å
Journal: Nat Microbiol / Year: 2022 Title: Structure of a thylakoid-anchored contractile injection system in multicellular cyanobacteria. Authors: Gregor L Weiss / Fabian Eisenstein / Ann-Katrin Kieninger / Jingwei Xu / Hannah A Minas / Milena Gerber / Miki Feldmüller / Iris Maldener / Karl Forchhammer / Martin Pilhofer / Abstract: Contractile injection systems (CISs) mediate cell-cell interactions by phage tail-like structures, using two distinct modes of action: extracellular CISs are released into the medium, while type 6 ...Contractile injection systems (CISs) mediate cell-cell interactions by phage tail-like structures, using two distinct modes of action: extracellular CISs are released into the medium, while type 6 secretion systems (T6SSs) are attached to the cytoplasmic membrane and function upon cell-cell contact. Here, we characterized a CIS in the multicellular cyanobacterium Anabaena, with features distinct from extracellular CISs and T6SSs. Cryo-electron tomography of focused ion beam-milled cells revealed that CISs were anchored in thylakoid membrane stacks, facing the cell periphery. Single particle cryo-electron microscopy showed that this unique in situ localization was mediated by extensions of tail fibre and baseplate components. On stress, cyanobacteria induced the formation of ghost cells, presenting thylakoid-anchored CISs to the environment. Functional assays suggest that these CISs may mediate ghost cell formation and/or interactions of ghost cells with other organisms. Collectively, these data provide a framework for understanding the evolutionary re-engineering of CISs and potential roles of these CISs in cyanobacterial programmed cell death.
History
Deposition
Dec 3, 2020
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Header (metadata) release
Feb 23, 2022
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Map release
Feb 23, 2022
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Update
Mar 16, 2022
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Current status
Mar 16, 2022
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Model: Quantifoil / Support film - Material: CARBON / Support film - topology: CONTINUOUS
Vitrification
Cryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV
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Electron microscopy
Microscope
FEI TITAN KRIOS
Image recording
Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 4 / Number real images: 19000 / Average electron dose: 52.0 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
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