[English] 日本語

- PDB-9nh0: In situ cryo-EM structure of PR and DotA-IcmX of the Legionella D... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 9nh0 | ||||||
---|---|---|---|---|---|---|---|
Title | In situ cryo-EM structure of PR and DotA-IcmX of the Legionella Dot/Icm T4SS machine at C1 symmetry | ||||||
![]() |
| ||||||
![]() | PROTEIN TRANSPORT / Type IVB Dot/Icm Secretion Machine | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.63 Å | ||||||
![]() | Yue, J. / Liu, J. | ||||||
Funding support | ![]()
| ||||||
![]() | ![]() Title: structures of the Dot/Icm T4SS identify the DotA-IcmX complex as the gatekeeper for effector translocation. Authors: Jian Yue / Samira Heydari / Donghyun Park / David Chetrit / Shoichi Tachiyama / Wangbiao Guo / Jack M Botting / Shenping Wu / Craig R Roy / Jun Liu Abstract: The Dot/Icm machine in is one of the most versatile type IV secretion systems (T4SSs), with a remarkable capacity to translocate over 330 different effector proteins across the bacterial envelope ...The Dot/Icm machine in is one of the most versatile type IV secretion systems (T4SSs), with a remarkable capacity to translocate over 330 different effector proteins across the bacterial envelope into host cells. At least 27 Dot and Icm proteins are required for assembly and function of the system, yet the architecture and activation mechanism remain poorly understood at the molecular level. Here, we deploy cryo-electron microscopy to reveal structures of the Dot/Icm machine at near-atomic resolution. Importantly, two proteins essential for effector translocation, DotA and IcmX, form a pentameric protochannel at an inactive state. Upon activation, the DotA-IcmX protochannel undergoes extensive rearrangements to form an extended transenvelope passage capable of transporting effector proteins from the bacterial cytoplasm into host cells as revealed by cryo-electron tomography. Collectively, our findings suggest that the DotA-IcmX complex functions as the gatekeeper for effector translocation of the Dot/Icm T4SS. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 2.8 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.8 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 3.4 MB | Display | |
Data in XML | ![]() | 378.8 KB | Display | |
Data in CIF | ![]() | 571.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 49398MC ![]() 9nguC ![]() 9ngvC ![]() 9ngwC ![]() 9ngyC ![]() 9nh1C ![]() 9nh2C M: map data used to model this data C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
-
Assembly
Deposited unit | ![]()
|
---|---|
1 |
|
-
Components
-Unknown peptide ... , 4 types, 72 molecules AaAgAmAsAyBeBkBqBwCcCiCoCuDaDgDmDsDyAbAhAnAtAzBfBlBrBxCdCjCp...
#1: Protein/peptide | Mass: 1679.849 Da / Num. of mol.: 18 / Source method: isolated from a natural source Source: (natural) ![]() #2: Protein/peptide | Mass: 910.095 Da / Num. of mol.: 18 / Source method: isolated from a natural source Source: (natural) ![]() #3: Protein/peptide | Mass: 1775.978 Da / Num. of mol.: 18 / Source method: isolated from a natural source Source: (natural) ![]() #4: Protein/peptide | Mass: 505.521 Da / Num. of mol.: 18 / Source method: isolated from a natural source Source: (natural) ![]() |
---|
-Protein , 5 types, 69 molecules AeAkAqAwBcBiBoBuCaCgCmCsCyDeDkDqDwEcAfAlArAxBdBjBpBvCbChCnCt...
#5: Protein | Mass: 29729.969 Da / Num. of mol.: 18 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q5ZYC0 #6: Protein | Mass: 38958.926 Da / Num. of mol.: 18 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q5ZYC2 #7: Protein | Mass: 107911.891 Da / Num. of mol.: 23 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q5ZYC1 #8: Protein | Mass: 50712.422 Da / Num. of mol.: 5 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q5ZS30 #9: Protein | Mass: 113235.570 Da / Num. of mol.: 5 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: Q5ZS33 |
---|
-Details
Has protein modification | Y |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: CELL / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
Component | Name: PR-protoChannel / Type: COMPLEX / Entity ID: all / Source: NATURAL |
---|---|
Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() |
Buffer solution | pH: 6.7 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy imaging
Microscopy | Model: FEI TECNAI 12 |
---|---|
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
Image recording | Electron dose: 73 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-
Processing
EM software | Name: PHENIX / Version: 1.21.2_5419 / Category: model refinement | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
3D reconstruction | Resolution: 4.63 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 37503 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 260.1 Å2 | ||||||||||||||||||||||||
Refine LS restraints |
|