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Yorodumi- EMDB-11747: Cryo-EM structure of an extracellular contractile injection syste... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-11747 | ||||||||||||
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Title | Cryo-EM structure of an extracellular contractile injection system in marine bacterium Algoriphagus machipongonensis, the contracted sheath shell. | ||||||||||||
Map data | |||||||||||||
Sample |
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Keywords | extracellular contractile injection system / STRUCTURAL PROTEIN | ||||||||||||
Function / homology | : / Tail sheath protein, C-terminal domain / Phage tail sheath C-terminal domain / Putative phage tail sheath protein FI Function and homology information | ||||||||||||
Biological species | Algoriphagus machipongonensis (bacteria) | ||||||||||||
Method | helical reconstruction / cryo EM / Resolution: 2.5 Å | ||||||||||||
Authors | Xu J / Ericson C | ||||||||||||
Funding support | Switzerland, 3 items
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Citation | Journal: Nat Microbiol / Year: 2022 Title: Identification and structure of an extracellular contractile injection system from the marine bacterium Algoriphagus machipongonensis. Authors: Jingwei Xu / Charles F Ericson / Yun-Wei Lien / Florentine U N Rutaganira / Fabian Eisenstein / Miki Feldmüller / Nicole King / Martin Pilhofer / Abstract: Contractile injection systems (CISs) are phage tail-like nanomachines, mediating bacterial cell-cell interactions as either type VI secretion systems (T6SSs) or extracellular CISs (eCISs). ...Contractile injection systems (CISs) are phage tail-like nanomachines, mediating bacterial cell-cell interactions as either type VI secretion systems (T6SSs) or extracellular CISs (eCISs). Bioinformatic studies uncovered a phylogenetic group of hundreds of putative CIS gene clusters that are highly diverse and widespread; however, only four systems have been characterized. Here we studied a putative CIS gene cluster in the marine bacterium Algoriphagus machipongonensis. Using an integrative approach, we show that the system is compatible with an eCIS mode of action. Our cryo-electron microscopy structure revealed several features that differ from those seen in other CISs: a 'cap adaptor' located at the distal end, a 'plug' exposed to the tube lumen, and a 'cage' formed by massive extensions of the baseplate. These elements are conserved in other CISs, and our genetic tools identified that they are required for assembly, cargo loading and function. Furthermore, our atomic model highlights specific evolutionary hotspots and will serve as a framework for understanding and re-engineering CISs. | ||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_11747.map.gz | 130.8 MB | EMDB map data format | |
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Header (meta data) | emd-11747-v30.xml emd-11747.xml | 11.9 KB 11.9 KB | Display Display | EMDB header |
Images | emd_11747.png | 68.3 KB | ||
Filedesc metadata | emd-11747.cif.gz | 5.3 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-11747 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-11747 | HTTPS FTP |
-Validation report
Summary document | emd_11747_validation.pdf.gz | 593.9 KB | Display | EMDB validaton report |
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Full document | emd_11747_full_validation.pdf.gz | 593.5 KB | Display | |
Data in XML | emd_11747_validation.xml.gz | 7.5 KB | Display | |
Data in CIF | emd_11747_validation.cif.gz | 8.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11747 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-11747 | HTTPS FTP |
-Related structure data
Related structure data | 7aekMC 7adzC 7ae0C 7aebC 7aefC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_11747.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : The contracted sheath shell of an extracellular contractile injec...
Entire | Name: The contracted sheath shell of an extracellular contractile injection system in marine bacterium Algoriphagus machipongonensis. |
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Components |
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-Supramolecule #1: The contracted sheath shell of an extracellular contractile injec...
Supramolecule | Name: The contracted sheath shell of an extracellular contractile injection system in marine bacterium Algoriphagus machipongonensis. type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Algoriphagus machipongonensis (bacteria) |
-Macromolecule #1: Putative phage tail sheath protein FI
Macromolecule | Name: Putative phage tail sheath protein FI / type: protein_or_peptide / ID: 1 Details: the residues 288-320aa are not built up in the model due to the poor map density, with residues 430-446aa assigned by poly-alanine chain. Number of copies: 18 / Enantiomer: LEVO |
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Source (natural) | Organism: Algoriphagus machipongonensis (bacteria) |
Molecular weight | Theoretical: 76.319039 KDa |
Sequence | String: MATYKTPGVY IEEITKFPPS VAQVETAIPA FIGYTQFART KPSVDSDDLI LKPKRISSLL DFTTYYGGAQ NEQGITVKLT DTLIEGAEN RTINVPEPTF KSPYLMFYSL QMYFANGGGP CYIVSTGVYD DWSDSETPPT INFSDLESGL AVIRKEDEPT L LLFPDATN ...String: MATYKTPGVY IEEITKFPPS VAQVETAIPA FIGYTQFART KPSVDSDDLI LKPKRISSLL DFTTYYGGAQ NEQGITVKLT DTLIEGAEN RTINVPEPTF KSPYLMFYSL QMYFANGGGP CYIVSTGVYD DWSDSETPPT INFSDLESGL AVIRKEDEPT L LLFPDATN LPTDDEFYSL YNSALMQCND LQDRFTILDT YSDQTYNDGV EDLDPIPALR NGINLTKDYL KYGAAYYPFV QT ILNYQYS ADEIVIQHLS YNPNAIATAL DNLNAVNGPT FIDAILDDLR DLSLPDISGE ISDAVGFMYD DVDGFDIDGT FTT NSVKVA NFASLVESVL STLNELIDAK EEINKDVNSA IASSEEDNAI KTAISDALDV FNEDFEGADK IESVAKNLSD LLIK IKQAD TNTKVENVLS INALNFSAEF EKLLTYDVNT GLTASVTLDL FANIGTRLDD IIAAVSAAEP IDVNNGKLNG RLLSD IEPL DNATYNTILL EINSHKVTLP PSSSMAGAYA RVDNDRGVWK SPANIGLNYV SKPSVTVSHE EQESMNVHGT GKSVNA IRS FVGKGTLVWG ARTLAGNDNE WRYISVRRFF NMAEESIKKA TEQFVFEPND GNTWVRVRAM IENFLILQWR AGALAGA KP EHAFYVKVGL GQTMTAQDIL EGNMNVEIGL AVVRPAEFII LKFSHKMQES UniProtKB: Putative phage tail sheath protein FI |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | helical reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE-PROPANE / Instrument: FEI VITROBOT MARK IV |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Final reconstruction | Applied symmetry - Helical parameters - Δz: 18.04 Å Applied symmetry - Helical parameters - Δ&Phi: 32.20 ° Applied symmetry - Helical parameters - Axial symmetry: C6 (6 fold cyclic) Resolution.type: BY AUTHOR / Resolution: 2.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 92922 |
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Startup model | Type of model: EMDB MAP EMDB ID: |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: AB INITIO MODEL |
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Output model | PDB-7aek: |