[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleIn situ structures of the Dot/Icm T4SS identify the DotA-IcmX complex as the gatekeeper for effector translocation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 39, Page e2516300122, Year 2025
Publish dateSep 30, 2025
AuthorsJian Yue / Samira Heydari / Donghyun Park / David Chetrit / Shoichi Tachiyama / Wangbiao Guo / Jack M Botting / Shenping Wu / Craig R Roy / Jun Liu /
PubMed AbstractThe Dot/Icm machine of is among the most versatile type IV secretion systems (T4SSs), capable of translocating more than 330 distinct effector proteins across the bacterial envelope into host cells. ...The Dot/Icm machine of is among the most versatile type IV secretion systems (T4SSs), capable of translocating more than 330 distinct effector proteins across the bacterial envelope into host cells. Assembly and function of the system require at least 27 Dot and Icm proteins, yet its architecture and activation mechanism remain poorly understood at the molecular level. Here, we deploy in situ single-particle cryoelectron microscopy to determine near-atomic structures of the Dot/Icm machine and its intimate association with three distinct outer membrane porins in intact bacteria. Notably, two essential yet enigmatic components, DotA and IcmX, form a pentameric protochannel in an inactive state at the central axis of the Dot/Icm machine. Upon Dot/Icm activation with host lysate, this protochannel undergoes extensive rearrangements to generate an extended transenvelope conduit, as visualized by cryoelectron tomography (cryo-ET) and subtomogram averaging. Furthermore, a combination of cryo-ET and cryo-FIB milling of macrophages infected with reveals tethering of the Dot/Icm machine to the host membrane, suggesting direct translocation of effector proteins from the bacterial cytoplasm into the host. Together, our studies identify the DotA-IcmX complex as a gatekeeper for effector translocation and provide a molecular framework for understanding the assembly and activation of the elaborate Dot/Icm T4SS.
External linksProc Natl Acad Sci U S A / PubMed:40986344 / PubMed Central
MethodsEM (single particle)
Resolution2.96 - 4.63 Å
Structure data

EMDB-49393: In-situ cryo-EM structure of outer membrane cap (OMC) of the Dot/Icm machine
PDB-9ngu: In situ cryo-EM structure of outer membrane cap (OMC) of the Legionella Dot/Icm T4SS machine
Method: EM (single particle) / Resolution: 2.96 Å

EMDB-49394: In-situ cryo-EM structure of periplasmic ring (PR) of the Dot/Icm machine
PDB-9ngv: In situ cryo-EM structure of periplasmic ring (PR) of the Legionella Dot/Icm T4SS machine.
Method: EM (single particle) / Resolution: 3.04 Å

EMDB-49395: In-situ cryo-EM structure of Dome of the Dot/Icm machine
PDB-9ngw: In-situ cryo-EM structure of Dome of the Legionella Dot/Icm machine
PDB-9nh2: In situ cryo-EM structure of porin III of the Legionella Dot/Icm T4SS machine
Method: EM (single particle) / Resolution: 3.08 Å

EMDB-49396: In-situ cryo-EM structure of protochannel of the Dot/Icm machine
PDB-9ngy: In situ cryo-EM structure of protochannel (DotA-IcmX) of the Legionella Dot/Icm T4SS machine
Method: EM (single particle) / Resolution: 3.63 Å

EMDB-49398: In-situ cryo-EM structure of PR and DotA-IcmX of the Dot/Icm machine at C1
PDB-9nh0: In situ cryo-EM structure of PR and DotA-IcmX of the Legionella Dot/Icm T4SS machine at C1 symmetry
Method: EM (single particle) / Resolution: 4.63 Å

EMDB-49399: In-situ cryo-EM structure of porinI of the Dot/Icm machine
PDB-9nh1: In situ cryo-EM structure of porin I of the Legionella Dot/Icm T4SS machine
Method: EM (single particle) / Resolution: 3.56 Å

Source
  • legionella pneumophila subsp. pneumophila (bacteria)
KeywordsPROTEIN TRANSPORT / Type IVB Dot/Icm Secretion Machine

+
About Yorodumi Papers

-
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 Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more