Evidence map›Paper›PMID 28714967›Full record

ArticleNature microbiology2017

Architecture of the type IV coupling protein complex of Legionella pneumophila.

Mi-Jeong Kwak, J Dongun Kim, Hyunmin Kim, Cheolhee Kim, James W Bowman, Seonghoon Kim, Keehyoung Joo, Jooyoung Lee, Kyeong Sik Jin, Yeon-Gil Kim and 3 more

Abstract read
In one paragraph

Article in Nature microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
7.2field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

45 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. OptimizedMicrobiology spectrum · 2025
    Article
  8. Journal of bacteriology · 2024
    Review
  9. Article
  10. Article
  11. Membrane association and polar localization of theProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 4 institutions in 2 countries.

Mi-Jeong KwakDepartment of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon 34141, Korea.
J Dongun KimDepartment of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon 34141, Korea.
Hyunmin KimDepartment of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon 34141, Korea.
Cheolhee KimDepartment of Physics, Pohang University of Science and Technology, Pohang, Kyungbuk 37673, Korea.
James W BowmanDepartment of Molecular Microbiology and Immunology, Keck School of Medicine, University of Southern California, 1975 Zonal Avenue, Los Angeles, California 90033, USA.
Seonghoon KimDepartment of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon 34141, Korea.
Keehyoung JooCenter for Advanced Computation, School of Computational Sciences, Korea Institute for Advanced Study, Seoul 02455, Korea.
Jooyoung LeeCenter for Advanced Computation, School of Computational Sciences, Korea Institute for Advanced Study, Seoul 02455, Korea.
Kyeong Sik JinPohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Kyungbuk 37673, Korea.
Yeon-Gil KimPohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Kyungbuk 37673, Korea.
Nam Ki LeeDepartment of Physics, Pohang University of Science and Technology, Pohang, Kyungbuk 37673, Korea.ORCID http://orcid.org/0000-0002-6597-555X
Jae U JungDepartment of Molecular Microbiology and Immunology, Keck School of Medicine, University of Southern California, 1975 Zonal Avenue, Los Angeles, California 90033, USA.
Byung-Ha OhDepartment of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon 34141, Korea.ORCID http://orcid.org/0000-0002-6437-8470
Korea Advanced Institute of Science and Technology · KRPohang University of Science and Technology · KRKorea Institute for Advanced Study · KRUniversity of Southern California · US

Funding

DOCTORAL AND POST-DOCTORAL TRAINING IN CRANIOFACIAL BIOLOGYT90DE021982 · NIDCR · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PAINE, MICHAEL LANSDELL · 2011 to 2025
$6.2M
Molecular Basis of KSHV oncogenesisR35CA200422 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI JUNG, JAE U · 2016 to 2022
$6.1M
NCI NIH HHS R35 CA200422NIDCR NIH HHS T90 DE021982
6 · The paper itself

Abstract

Many bacteria, including Legionella pneumophila, rely on the type IV secretion system to translocate a repertoire of effector proteins into the hosts for their survival and growth. Type IV coupling protein (T4CP) is a hexameric ATPase that links translocating substrates to the transenvelope secretion conduit. Yet, how a large number of effector proteins are selectively recruited and processed by T4CPs remains enigmatic. DotL, the T4CP of L. pneumophila, contains an ATPase domain and a C-terminal extension whose function is unknown. Unlike T4CPs involved in plasmid DNA translocation, DotL appeared to function by forming a multiprotein complex with four other proteins. Here, we show that the C-terminal extension of DotL interacts with DotN, IcmS, IcmW and an additionally identified subunit LvgA, and that this pentameric assembly binds Legionella effector proteins. We determined the crystal structure of this assembly and built an architecture of the T4CP holocomplex by combining a homology model of the ATPase domain of DotL. The holocomplex is a hexamer of a bipartite structure composed of a membrane-proximal ATPase domain and a membrane-distal substrate-recognition assembly. The presented information demonstrates the architecture and functional dissection of the multiprotein T4CP complexes and provides important insights into their substrate recruitment and processing.

Indexed as

Bacterial ProteinsCrystallography, X-RayGene Expression Regulation, BacterialLegionella pneumophilaModels, MolecularMultiprotein ComplexesProtein DomainsType IV Secretion SystemsBacterial ProteinsDotL protein, Legionella pneumophilaMultiprotein ComplexesType IV Secretion Systems

Identifiers

PMID28714967
PMCPMC6497169
OpenAlexW2734584123

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.