Evidence map›Paper›PMID 38321146›Full record

ArticleNature structural & molecular biology2024

Activation of CBASS Cap5 endonuclease immune effector by cyclic nucleotides.

Olga Rechkoblit, Daniela Sciaky, Dale F Kreitler, Angeliki Buku, Jithesh Kottur, Aneel K Aggarwal

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
  2. Crystal structure of the cytosolic Nudix-like domain of CD-NTase-associated protein 16 from Enterococcus faecalis.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
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  11. 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

6 authors.

Olga RechkoblitDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA. olga.rechkoblit@mssm.edu.ORCID http://orcid.org/0000-0003-4270-7242
Daniela SciakyDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID http://orcid.org/0009-0000-3182-9493
Dale F KreitlerCenter for BioMolecular Structure NSLS‑II, Brookhaven National Laboratory, Upton, NY, USA.
Angeliki BukuDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA.
Jithesh KotturDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA.ORCID http://orcid.org/0000-0002-8075-3883
Aneel K AggarwalDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, USA. aneel.aggarwal@mssm.edu.ORCID http://orcid.org/0000-0003-4389-0173

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
Structure and Specificity of Restriction-Modification (R-M) SystemsR35GM131780 · NIGMS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI ANEEL K. AGGARWAL · 2019 to 2026
$3.4M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
NIGMS NIH HHS P30 GM124165NIGMS NIH HHS P41 GM103310NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R35 GM131780NIH HHS S10 OD021527
6 · The paper itself

Abstract

The bacterial cyclic oligonucleotide-based antiphage signaling system (CBASS) is similar to the cGAS-STING system in humans, containing an enzyme that synthesizes a cyclic nucleotide on viral infection and an effector that senses the second messenger for the antiviral response. Cap5, containing a SAVED domain coupled to an HNH DNA endonuclease domain, is the most abundant CBASS effector, yet the mechanism by which it becomes activated for cell killing remains unknown. We present here high-resolution structures of full-length Cap5 from Pseudomonas syringae (Ps) with second messengers. The key to PsCap5 activation is a dimer-to-tetramer transition, whereby the binding of second messenger to dimer triggers an open-to-closed transformation of the SAVED domains, furnishing a surface for assembly of the tetramer. This movement propagates to the HNH domains, juxtaposing and converting two HNH domains into states for DNA destruction. These results show how Cap5 effects bacterial cell suicide and we provide proof-in-principle data that the CBASS can be extrinsically activated to limit bacterial infections.

Indexed as

Bacterial ProteinsEndonucleasesPseudomonas syringaeApoproteinsBacteriophagesDinucleoside PhosphatesDNAEnzyme ActivationLigandsModels, ChemicalNucleotides, CyclicApoproteinsBacterial Proteinscyclic diadenosine phosphatecyclic guanosine monophosphate-adenosine monophosphateDinucleoside PhosphatesDNAEndonucleasesLigandsNucleotides, Cyclic

Identifiers

PMID38321146
PMCPMC11849724

What OpenQuestion holds

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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.