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- 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) | |||||||||
![]() | C17 reconstruction for Outer Membrane Core Complex (OMCC) of Type IV Secretion System (T4SS) encoded by F-plasmid (pED208) | |||||||||
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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![]() | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.95 Å | |||||||||
![]() | Liu X / Khara P / Baker ML / Christie PJ / Hu B | |||||||||
Funding support | ![]()
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![]() | ![]() Title: 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: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 218.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 8.4 KB 8.4 KB | Display Display | ![]() |
Images | ![]() | 150 KB | ||
Archive directory | ![]() ![]() | 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 | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | C17 reconstruction for Outer Membrane Core Complex (OMCC) of Type IV Secretion System (T4SS) encoded by F-plasmid (pED208) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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![]() | 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: ![]() |
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 |