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Yorodumi- EMDB-24770: C17 reconstruction for Outer Membrane Core Complex (OMCC) of Type... -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-24770 | |||||||||
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| Title | C17 reconstruction for Outer Membrane Core Complex (OMCC) of Type IV Secretion System (T4SS) encoded by F-plasmid (pED208) | |||||||||
Map data | C17 reconstruction for Outer Membrane Core Complex (OMCC) of Type IV Secretion System (T4SS) encoded by F-plasmid (pED208) | |||||||||
Sample |
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| Function / homology | Type IV conjugative transfer system protein TraV / Type IV conjugative transfer system lipoprotein (TraV) / Bacterial conjugation TrbI-like protein / Type IV secretion system, VirB10 / TraB / TrbI / Prokaryotic membrane lipoprotein lipid attachment site profile. / TraV / TraB Function and homology information | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.95 Å | |||||||||
Authors | Liu X / Khara P / Baker ML / Christie PJ / Hu B | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Nat Commun / Year: 2022Title: Structure of a type IV secretion system core complex encoded by multi-drug resistance F plasmids. Authors: Xiangan Liu / Pratick Khara / Matthew L Baker / Peter J Christie / Bo Hu / ![]() Abstract: Bacterial type IV secretion systems (T4SSs) are largely responsible for the proliferation of multi-drug resistance. We solved the structure of the outer-membrane core complex (OMCC) of a T4SS encoded ...Bacterial type IV secretion systems (T4SSs) are largely responsible for the proliferation of multi-drug resistance. We solved the structure of the outer-membrane core complex (OMCC) of a T4SS encoded by a conjugative F plasmid at <3.0 Å resolution by cryoelectron microscopy. The OMCC consists of a 13-fold symmetrical outer ring complex (ORC) built from 26 copies of TraK and TraV C-terminal domains, and a 17-fold symmetrical central cone (CC) composed of 17 copies of TraB β-barrels. Domains of TraV and TraB also bind the CC and ORC substructures, establishing that these proteins undergo an intraprotein symmetry alteration to accommodate the C13:C17 symmetry mismatch. We present evidence that other pED208-encoded factors stabilize the C13:C17 architecture and define the importance of TraK, TraV and TraB domains to T4SS function. This work identifies OMCC structural motifs of proposed importance for structural transitions associated with F plasmid dissemination and F pilus biogenesis. | |||||||||
| History |
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_24770.map.gz | 218.1 MB | EMDB map data format | |
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| Header (meta data) | emd-24770-v30.xml emd-24770.xml | 8.4 KB 8.4 KB | Display Display | EMDB header |
| Images | emd_24770.png | 150 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-24770 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-24770 | HTTPS FTP |
-Validation report
| Summary document | emd_24770_validation.pdf.gz | 327.6 KB | Display | EMDB validaton report |
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| Full document | emd_24770_full_validation.pdf.gz | 327.1 KB | Display | |
| Data in XML | emd_24770_validation.xml.gz | 7.2 KB | Display | |
| Data in CIF | emd_24770_validation.cif.gz | 8.2 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-24770 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-24770 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7spcMC ![]() 7spbC ![]() 7spiC ![]() 7spjC ![]() 7spkC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_24770.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | C17 reconstruction for Outer Membrane Core Complex (OMCC) of Type IV Secretion System (T4SS) encoded by F-plasmid (pED208) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.0652 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Outer membrane core complex of T4SS encoded by plasmid pED208
| Entire | Name: Outer membrane core complex of T4SS encoded by plasmid pED208 |
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| Components |
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-Supramolecule #1: Outer membrane core complex of T4SS encoded by plasmid pED208
| Supramolecule | Name: Outer membrane core complex of T4SS encoded by plasmid pED208 type: organelle_or_cellular_component / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: ![]() |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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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: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 40.0 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 |
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Image processing
| CTF correction | Software - Name: cryoSPARC |
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| Final reconstruction | Applied symmetry - Point group: C17 (17 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 2.95 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 70700 |
| Initial angle assignment | Type: NOT APPLICABLE |
| Final angle assignment | Type: PROJECTION MATCHING / Software - Name: cryoSPARC |
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