Evidence map›Paper›PMID 22063095›Full record

ArticleJournal of molecular biology2012

Domain flexibility modulates the heterogeneous assembly mechanism of anthrax toxin protective antigen.

Geoffrey K Feld, Alexander F Kintzer, Iok I Tang, Katie L Thoren, Bryan A Krantz

Abstract read
In one paragraph

Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Recombinant full-lengthFrontiers in immunology · 2022
    Article
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  15. Review
  16. Ratcheting up protein translocation with anthrax toxin.Protein science : a publication of the Protein Society · 2012
    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

5 authors at 1 institution in 1 country.

Geoffrey K FeldDepartment of Chemistry, University of California, Berkeley, CA 94720, USA.
Alexander F Kintzer
Iok I Tang
Katie L Thoren
Bryan A Krantz
University of California, Berkeley · US

Funding

Physical Principles of Bacterial Toxin Translocation across MembranesR01AI077703 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI KRANTZ, BRYAN ANDREW · 2008 to 2017
$3.3M
NIAID NIH HHS R01 AI077703NIAID NIH HHS R01-AI077703
6 · The paper itself

Abstract

The three protein components of anthrax toxin are nontoxic individually, but they form active holotoxin complexes upon assembly. The role of the protective antigen (PA) component of the toxin is to deliver two other enzyme components, lethal factor and edema factor, across the plasma membrane and into the cytoplasm of target cells. PA is produced as a proprotein, which must be proteolytically activated; generally, cell surface activation is mediated by a furin family protease. Activated PA can then assemble into one of two noninterconverting oligomers, a homoheptamer and a homooctamer, which have unique properties. Herein we describe molecular determinants that influence the stoichiometry of PA in toxin complexes. By tethering PA domain 4 (D4) to domain 2 with two different-length cross-links, we can control the relative proportions of PA heptamers and octamers. The longer cross-link favors octamer formation, whereas the shorter one favors formation of the heptamer. X-ray crystal structures of PA (up to 1.45 Å resolution), including these cross-linked PA constructs, reveal that a hinge-like movement of D4 correlates with the relative preference for each oligomeric architecture. Furthermore, we report the conformation of the flexible loop containing the furin cleavage site and show that, for efficient processing, the furin site cannot be moved ~5 or 6 residues within the loop. We propose that there are different orientations of D4 relative to the main body of PA that favor the formation of either the heptamer or the octamer.

Indexed as

Antigens, BacterialBacillus anthracisBacterial ToxinsBinding SitesCell MembraneCrystallography, X-RayCytoplasmFurinModels, MolecularProtein Structure, SecondaryProtein Structure, Tertiaryanthrax toxinAntigens, BacterialBacterial ToxinsFurin

Identifiers

PMID22063095
PMCPMC3249527
OpenAlexW2105189356

What OpenQuestion holds

Textmetadata
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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.