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Yorodumi- EMDB-13859: L. pneumophila Type IV Coupling Complex (T4CC) computed from a sa... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-13859 | |||||||||
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Title | L. pneumophila Type IV Coupling Complex (T4CC) computed from a sample where dotY/Z genes were deleted (referred to as T4CCdeltaDotYZ at 15A) | |||||||||
Map data | DotLMN complex from DotYZ mutant - T4CCdeltaDotYZ at 15A | |||||||||
Sample |
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Keywords | Type IV Coupling Complex / T4CC / Type IV Secretion System / T4SS / Membrane protein complex / Membrane complex / DotY / DotZ / DotL / dotM / dotN / IcmSW / Legionella / MEMBRANE PROTEIN / delta DotY/Z | |||||||||
Function / homology | Function and homology information | |||||||||
Biological species | Legionella pneumophila (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 15.0 Å | |||||||||
Authors | Mace K / Meir A / Lukoyanova N / Waksman G | |||||||||
Funding support | European Union, 1 items
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Citation | Journal: Mol Microbiol / Year: 2022 Title: Proteins DotY and DotZ modulate the dynamics and localization of the type IVB coupling complex of Legionella pneumophila. Authors: Kevin Macé / Amit Meir / Natalya Lukoyanova / Luying Liu / David Chetrit / Manuela K Hospenthal / Craig R Roy / Gabriel Waksman / Abstract: Legionella pneumophila is an opportunistic pathogen infecting alveolar macrophages and protozoa species. Legionella utilizes a Type IV Secretion System (T4SS) to translocate over 300 effector ...Legionella pneumophila is an opportunistic pathogen infecting alveolar macrophages and protozoa species. Legionella utilizes a Type IV Secretion System (T4SS) to translocate over 300 effector proteins into its host cell. In a recent study, we have isolated and solved the cryo-EM structure of the Type IV Coupling Complex (T4CC), a large cytoplasmic determinant associated with the inner membrane that recruits effector proteins for delivery to the T4SS for translocation. The T4CC is composed of a DotLMNYZ hetero-pentameric core from which the flexible IcmSW module flexibly protrudes. The DotY and DotZ proteins were newly reported members of this complex and their role remained elusive. In this study, we observed the effect of deleting DotY and DotZ on T4CC stability and localization. Furthermore, we found these two proteins are co-dependent, whereby the deletion of DotY resulted in DotZ absence from the coupling complex, and vice versa. Additional cryo-EM data analysis revealed the dynamic movement of the IcmSW module is modified by the DotY/Z proteins. We therefore determined the likely function of DotY and DotZ and revealed their importance on T4CC function. | |||||||||
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_13859.map.gz | 15.2 MB | EMDB map data format | |
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Header (meta data) | emd-13859-v30.xml emd-13859.xml | 7.9 KB 7.9 KB | Display Display | EMDB header |
Images | emd_13859.png | 29.8 KB | ||
Filedesc metadata | emd-13859.cif.gz | 3.6 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-13859 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-13859 | HTTPS FTP |
-Validation report
Summary document | emd_13859_validation.pdf.gz | 287.1 KB | Display | EMDB validaton report |
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Full document | emd_13859_full_validation.pdf.gz | 286.7 KB | Display | |
Data in XML | emd_13859_validation.xml.gz | 6.5 KB | Display | |
Data in CIF | emd_13859_validation.cif.gz | 7.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13859 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13859 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_13859.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | DotLMN complex from DotYZ mutant - T4CCdeltaDotYZ at 15A | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.045 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 : DotLMN_IcmSW
Entire | Name: DotLMN_IcmSW |
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Components |
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-Supramolecule #1: DotLMN_IcmSW
Supramolecule | Name: DotLMN_IcmSW / type: complex / ID: 1 / Parent: 0 / Details: Heterogeneity from DotLMNYZ_IcmSW WT |
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Source (natural) | Organism: Legionella pneumophila (bacteria) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-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: 54.0 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
Startup model | Type of model: EMDB MAP EMDB ID: |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 15.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 50210 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |