[English] 日本語
Yorodumi
- PDB-9nh0: In situ cryo-EM structure of PR and DotA-IcmX of the Legionella D... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9nh0
TitleIn situ cryo-EM structure of PR and DotA-IcmX of the Legionella Dot/Icm T4SS machine at C1 symmetry
Components
  • (unknown peptide ...) x 4
  • DotA
  • IcmE (DotG)
  • IcmG (DotF)
  • IcmK (DotH)
  • IcmX (IcmY)
KeywordsPROTEIN TRANSPORT / Type IVB Dot/Icm Secretion Machine
Function / homology
Function and homology information


Phagosome trafficking protein DotA / Conjugal transfer/type IV secretion protein DotA/TraY / Phagosome trafficking protein DotA / : / : / Decapeptide repeat region / Putative outer membrane core complex of type IVb secretion / Putative outer membrane core complex of type IVb secretion / Type IV secretion system, VirB10/TrbI / Bacterial conjugation TrbI-like protein ...Phagosome trafficking protein DotA / Conjugal transfer/type IV secretion protein DotA/TraY / Phagosome trafficking protein DotA / : / : / Decapeptide repeat region / Putative outer membrane core complex of type IVb secretion / Putative outer membrane core complex of type IVb secretion / Type IV secretion system, VirB10/TrbI / Bacterial conjugation TrbI-like protein / Type IV secretion system, VirB10 / TraB / TrbI / Prokaryotic membrane lipoprotein lipid attachment site profile.
Similarity search - Domain/homology
IcmX (IcmY) / DotA / IcmG (DotF) / IcmE (DotG) / IcmK (DotH)
Similarity search - Component
Biological speciesLegionella pneumophila subsp. pneumophila (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.63 Å
AuthorsYue, J. / Liu, J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/Office of the DirectorR01AI152421 United States
CitationJournal: bioRxiv / Year: 2025
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
DepositionFeb 23, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 17, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
Aa: unknown peptide E
Ab: unknown peptide F
Ac: unknown peptide G
Ad: unknown peptide H
Ae: IcmG (DotF)
Af: IcmK (DotH)
Ag: unknown peptide E
Ah: unknown peptide F
Ai: unknown peptide G
Aj: unknown peptide H
Ak: IcmG (DotF)
Al: IcmK (DotH)
Am: unknown peptide E
An: unknown peptide F
Ao: unknown peptide G
Ap: unknown peptide H
Aq: IcmG (DotF)
Ar: IcmK (DotH)
As: unknown peptide E
At: unknown peptide F
Au: unknown peptide G
Av: unknown peptide H
Aw: IcmG (DotF)
Ax: IcmK (DotH)
Ay: unknown peptide E
Az: unknown peptide F
Ba: unknown peptide G
Bb: unknown peptide H
Bc: IcmG (DotF)
Bd: IcmK (DotH)
Be: unknown peptide E
Bf: unknown peptide F
Bg: unknown peptide G
Bh: unknown peptide H
Bi: IcmG (DotF)
Bj: IcmK (DotH)
Bk: unknown peptide E
Bl: unknown peptide F
Bm: unknown peptide G
Bn: unknown peptide H
Bo: IcmG (DotF)
Bp: IcmK (DotH)
Bq: unknown peptide E
Br: unknown peptide F
Bs: unknown peptide G
Bt: unknown peptide H
Bu: IcmG (DotF)
Bv: IcmK (DotH)
Bw: unknown peptide E
Bx: unknown peptide F
By: unknown peptide G
Bz: unknown peptide H
Ca: IcmG (DotF)
Cb: IcmK (DotH)
Cc: unknown peptide E
Cd: unknown peptide F
Ce: unknown peptide G
Cf: unknown peptide H
Cg: IcmG (DotF)
Ch: IcmK (DotH)
Ci: unknown peptide E
Cj: unknown peptide F
Ck: unknown peptide G
Cl: unknown peptide H
Cm: IcmG (DotF)
Cn: IcmK (DotH)
Co: unknown peptide E
Cp: unknown peptide F
Cq: unknown peptide G
Cr: unknown peptide H
Cs: IcmG (DotF)
Ct: IcmK (DotH)
Cu: unknown peptide E
Cv: unknown peptide F
Cw: unknown peptide G
Cx: unknown peptide H
Cy: IcmG (DotF)
Cz: IcmK (DotH)
Da: unknown peptide E
Db: unknown peptide F
Dc: unknown peptide G
Dd: unknown peptide H
De: IcmG (DotF)
Df: IcmK (DotH)
Dg: unknown peptide E
Dh: unknown peptide F
Di: unknown peptide G
Dj: unknown peptide H
Dk: IcmG (DotF)
Dl: IcmK (DotH)
Dm: unknown peptide E
Dn: unknown peptide F
Do: unknown peptide G
Dp: unknown peptide H
Dq: IcmG (DotF)
Dr: IcmK (DotH)
Ds: unknown peptide E
Dt: unknown peptide F
Du: unknown peptide G
Dv: unknown peptide H
Dw: IcmG (DotF)
Dx: IcmK (DotH)
Dy: unknown peptide E
Dz: unknown peptide F
Ea: unknown peptide G
Eb: unknown peptide H
Ec: IcmG (DotF)
Ed: IcmK (DotH)
Ee: IcmE (DotG)
Ef: IcmE (DotG)
Eg: IcmE (DotG)
Eh: IcmE (DotG)
Ei: IcmE (DotG)
Ej: IcmE (DotG)
Ek: IcmE (DotG)
El: IcmE (DotG)
Em: IcmE (DotG)
En: IcmE (DotG)
Eo: IcmE (DotG)
Ep: IcmE (DotG)
Eq: IcmE (DotG)
Er: IcmE (DotG)
Es: IcmE (DotG)
Et: IcmE (DotG)
Eu: IcmE (DotG)
Ev: IcmE (DotG)
Ew: IcmX (IcmY)
Ex: IcmX (IcmY)
Ey: IcmX (IcmY)
Ez: IcmX (IcmY)
Fa: IcmX (IcmY)
Fb: DotA
Fc: DotA
Fd: DotA
Fe: DotA
Ff: DotA
Fg: IcmE (DotG)
Fh: IcmE (DotG)
Fi: IcmE (DotG)
Fj: IcmE (DotG)
Fk: IcmE (DotG)


Theoretical massNumber of molelcules
Total (without water)4,625,800141
Polymers4,625,800141
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

-
Components

-
Unknown peptide ... , 4 types, 72 molecules AaAgAmAsAyBeBkBqBwCcCiCoCuDaDgDmDsDyAbAhAnAtAzBfBlBrBxCdCjCp...

#1: Protein/peptide
unknown peptide E


Mass: 1679.849 Da / Num. of mol.: 18 / Source method: isolated from a natural source
Source: (natural) Legionella pneumophila subsp. pneumophila (bacteria)
#2: Protein/peptide
unknown peptide F


Mass: 910.095 Da / Num. of mol.: 18 / Source method: isolated from a natural source
Source: (natural) Legionella pneumophila subsp. pneumophila (bacteria)
#3: Protein/peptide
unknown peptide G


Mass: 1775.978 Da / Num. of mol.: 18 / Source method: isolated from a natural source
Source: (natural) Legionella pneumophila subsp. pneumophila (bacteria)
#4: Protein/peptide
unknown peptide H


Mass: 505.521 Da / Num. of mol.: 18 / Source method: isolated from a natural source
Source: (natural) Legionella pneumophila subsp. pneumophila (bacteria)

-
Protein , 5 types, 69 molecules AeAkAqAwBcBiBoBuCaCgCmCsCyDeDkDqDwEcAfAlArAxBdBjBpBvCbChCnCt...

#5: Protein
IcmG (DotF)


Mass: 29729.969 Da / Num. of mol.: 18 / Source method: isolated from a natural source
Source: (natural) Legionella pneumophila subsp. pneumophila (bacteria)
References: UniProt: Q5ZYC0
#6: Protein
IcmK (DotH)


Mass: 38958.926 Da / Num. of mol.: 18 / Source method: isolated from a natural source
Source: (natural) Legionella pneumophila subsp. pneumophila (bacteria)
References: UniProt: Q5ZYC2
#7: Protein ...
IcmE (DotG)


Mass: 107911.891 Da / Num. of mol.: 23 / Source method: isolated from a natural source
Source: (natural) Legionella pneumophila subsp. pneumophila (bacteria)
References: UniProt: Q5ZYC1
#8: Protein
IcmX (IcmY)


Mass: 50712.422 Da / Num. of mol.: 5 / Source method: isolated from a natural source
Source: (natural) Legionella pneumophila subsp. pneumophila (bacteria)
References: UniProt: Q5ZS30
#9: Protein
DotA


Mass: 113235.570 Da / Num. of mol.: 5 / Source method: isolated from a natural source
Source: (natural) Legionella pneumophila subsp. pneumophila (bacteria)
References: UniProt: Q5ZS33

-
Details

Has protein modificationY

-
Experimental details

-
Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: CELL / 3D reconstruction method: single particle reconstruction

-
Sample preparation

ComponentName: PR-protoChannel / Type: COMPLEX / Entity ID: all / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Legionella pneumophila subsp. pneumophila (bacteria)
Buffer solutionpH: 6.7
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

-
Electron microscopy imaging

MicroscopyModel: FEI TECNAI 12
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 73 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

-
Processing

EM softwareName: PHENIX / Version: 1.21.2_5419 / Category: model refinement
CTF correctionType: PHASE FLIPPING ONLY
3D reconstructionResolution: 4.63 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 37503 / Symmetry type: POINT
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 260.1 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.005295926
ELECTRON MICROSCOPYf_angle_d1.2066130297
ELECTRON MICROSCOPYf_chiral_restr0.060514884
ELECTRON MICROSCOPYf_plane_restr0.00716764
ELECTRON MICROSCOPYf_dihedral_angle_d6.606413099

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more