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- EMDB-4876: Cryo-EM structure of the anti-feeding prophage (AFP) baseplate in... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-4876 | |||||||||
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Title | Cryo-EM structure of the anti-feeding prophage (AFP) baseplate in contracted state | |||||||||
![]() | None | |||||||||
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![]() | Anti-feeding prophage / secretion system / AFP / contractile / VIRUS LIKE PARTICLE / baseplate / contracted | |||||||||
Function / homology | Tail sheath protein, subtilisin-like domain / Phage tail sheath protein subtilisin-like domain / Tail sheath protein, C-terminal domain / Phage tail sheath C-terminal domain / Afp4 / Afp3 / Afp2![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 5.4 Å | |||||||||
![]() | Desfosses A | |||||||||
![]() | ![]() 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. | |||||||||
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 | ![]() | 74 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 14.5 KB 14.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.6 KB | Display | ![]() |
Images | ![]() | 96.6 KB | ||
Filedesc metadata | ![]() | 6.1 KB | ||
Others | ![]() ![]() | 100.5 MB 100.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 518.5 KB | Display | ![]() |
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Full document | ![]() | 518 KB | Display | |
Data in XML | ![]() | 12.6 KB | Display | |
Data in CIF | ![]() | 16.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6rglMC ![]() 4782C ![]() 4783C ![]() 4784C ![]() 4800C ![]() 4801C ![]() 4802C ![]() 4803C ![]() 4859C ![]() 4871C ![]() 6raoC ![]() 6rapC ![]() 6rbkC ![]() 6rbnC ![]() 6rc8C C: citing same article ( M: atomic model generated by this map |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | None | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.397 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Supplemental map: emd 4876 half map 1.map
File | emd_4876_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Supplemental map: emd 4876 half map 2.map
File | emd_4876_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-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 |
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Components |
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-Supramolecule #1: Cryo-EM structure of the anti-feeding prophage (AFP) baseplate in...
Supramolecule | Name: Cryo-EM structure of the anti-feeding prophage (AFP) baseplate in contracted state type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Afp2
Macromolecule | Name: Afp2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 38.784355 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MTVTTTYPGV YLSEDAVSSF SVNSAATAVP LFAYDSENTN TINKPIQVFR NWAEFTVEYP TPLEDAFYTS LSLWFMHGGG KCYLVNEAN IADAVAQYDD ITLIVAAGTD TTTYTAFTTV VGQGYRIFGL FDGPKEKIAG TAKPDEVMEE YPTSPFGAVF Y PWGTLASG ...String: MTVTTTYPGV YLSEDAVSSF SVNSAATAVP LFAYDSENTN TINKPIQVFR NWAEFTVEYP TPLEDAFYTS LSLWFMHGGG KCYLVNEAN IADAVAQYDD ITLIVAAGTD TTTYTAFTTV VGQGYRIFGL FDGPKEKIAG TAKPDEVMEE YPTSPFGAVF Y PWGTLASG AAVPPSAIAA ASITQTDRTR GVWKAPANQA VNGVTPAFAV SDDFQGKYNQ GKALNMIRTF SGQGTVVWGA RT LEDSDNW RYIPVRRLFN AVERDIQKSL NKLVFEPNSQ PTWQRVKAAV DSYLHSLWQQ GALAGNTPAD AWFVQVGKDL TMT QEEINQ GKMIIKIGLA AVRPAEFIIL QFSQDIAQ UniProtKB: Afp2 |
-Macromolecule #2: Afp3
Macromolecule | Name: Afp3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 48.777566 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MATVTSVPGV YIEEDASPAM SVSASATAVP LFVARFTPLK PELAGVITRI GSWLDYTILF DSNVPSSARV TVSSTAVEPS PEFDALETA SSKATTTYTY QIDDTEVVDP TASVALRLYF QNGGGPCYLY PLEKADDNGP LAALPDLIDE VGEITLLASP D PDETYRTA ...String: MATVTSVPGV YIEEDASPAM SVSASATAVP LFVARFTPLK PELAGVITRI GSWLDYTILF DSNVPSSARV TVSSTAVEPS PEFDALETA SSKATTTYTY QIDDTEVVDP TASVALRLYF QNGGGPCYLY PLEKADDNGP LAALPDLIDE VGEITLLASP D PDETYRTA VYGALAASLD QHKGYFLLAD SVNGDAPSAV GGSAQVAVYY PNVEVPHTRK LDDAEVAIDG YLDDEGKAVT TL AALRVVN TEFAGEIAQS LSGDLSAPLS LPPSALIAGV YGKTDGERGV WKAPANVVLN GVSDVSVRVT NEQQAELNPK GIN VIRHFS DRGLVVWGSR TQKDDDDWRY IPVRRLFDAA ERDIKKALQP MVFEPNSQLT WKRVQTAIDN YLYRLWQQGA LAGN KAEEA YFVRVGKGIT MTQDEINQGK MIIQVGMAAV RPAEFIILKF TQDMSQ UniProtKB: Afp3 |
-Macromolecule #3: Afp4
Macromolecule | Name: Afp4 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 45.565633 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MTMVLPGVSY NETLLTQASN DDPVTMPLFI GYTPPDTAIP VTVMQPVSVG SLTQANSLFG QRGTLAYSLR HFFENGGLQC YVLPLGPGK GEPAARLQEL IAALQTPQML ETLLADDKTG LVLVPELSEL NEVSSTSLSA EGVDAAEVDA DALWYQGWQV L LTLCRQAP ...String: MTMVLPGVSY NETLLTQASN DDPVTMPLFI GYTPPDTAIP VTVMQPVSVG SLTQANSLFG QRGTLAYSLR HFFENGGLQC YVLPLGPGK GEPAARLQEL IAALQTPQML ETLLADDKTG LVLVPELSEL NEVSSTSLSA EGVDAAEVDA DALWYQGWQV L LTLCRQAP QRFALLELPE DPASAVTLTQ QSFSADQCQR GAAWWPRLET SYQDESSAPV VLSPLPAVAA AIQRSAHDNG VW KAPANIA LAKTRRPTQS ILTSQALLDN QGVSCNLIRS FVGKGVRLWG CRTLLNEENT AWRYIQIRLL VSSVEHYLSK LAR AYLFEP NTAPTWMKLK GQVWTWLRQQ WLAGAFFGTV EDEAFSLSIG LDETMTEDDI RHGKMILQVR LALLAPAEFI AISL TLDLR DGTASAQTGG QS UniProtKB: Afp4 |
-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 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 27.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |