Evidence map›Paper›PMID 21037566›Full record

ArticleNature structural & molecular biology2010

Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers.

Geoffrey K Feld, Katie L Thoren, Alexander F Kintzer, Harry J Sterling, Iok I Tang, Shoshana G Greenberg, Evan R Williams, Bryan A Krantz

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

86 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Protective antigen-mediated delivery of an anti-CRISPR protein for precision genome editing.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Targeting the Inside of Cells with Biologicals: Toxin Routes in a Therapeutic Context.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article

26 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 1 country.

Geoffrey K FeldDepartment of Chemistry, University of California, Berkeley, California, USA.
Katie L Thoren
Alexander F Kintzer
Harry J Sterling
Iok I Tang
Shoshana G Greenberg
Evan R Williams
Bryan A Krantz
University of California, Berkeley · USQB3 · US

Funding

Physical Principles of Bacterial Toxin Translocation across MembranesR01AI077703 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI KRANTZ, BRYAN ANDREW · 2008 to 2017
$3.3M
Protein Conformation and Noncovalent InteractionsR01GM064712 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2002 to 2009
$2.0M
NIAID NIH HHS R01 AI077703NIAID NIH HHS R01-AI077703NIGMS NIH HHS R01 GM064712NIGMS NIH HHS R01-GM064712
6 · The paper itself

Abstract

The protein transporter anthrax lethal toxin is composed of protective antigen (PA), a transmembrane translocase, and lethal factor (LF), a cytotoxic enzyme. After its assembly into holotoxin complexes, PA forms an oligomeric channel that unfolds LF and translocates it into the host cell. We report the crystal structure of the core of a lethal toxin complex to 3.1-Å resolution; the structure contains a PA octamer bound to four LF PA-binding domains (LF(N)). The first α-helix and β-strand of each LF(N) unfold and dock into a deep amphipathic cleft on the surface of the PA octamer, which we call the α clamp. The α clamp possesses nonspecific polypeptide binding activity and is functionally relevant to efficient holotoxin assembly, PA octamer formation, and LF unfolding and translocation. This structure provides insight into the mechanism of translocation-coupled protein unfolding.

Indexed as

Protein UnfoldingAntigens, BacterialBacillus anthracisBacterial ToxinsBinding SitesModels, MolecularProtein Interaction MappingProtein Structure, TertiaryProtein TransportStructure-Activity Relationshipanthrax toxinAntigens, BacterialBacterial Toxins

Identifiers

PMID21037566
PMCPMC3133606
OpenAlexW1990289389

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.