Evidence map›Paper›PMID 40950076›Full record

ArticlebioRxiv : the preprint server for biology2025

Structural basis of QueC-family protein function in qatABCD anti-phage defense.

Angela Gao, Douglas R Wassarman, Philip J Kranzusch

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Angela GaoDepartment of Microbiology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0009-0002-7149-9841
Douglas R WassarmanDepartment of Microbiology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-6922-9378
Philip J KranzuschDepartment of Microbiology, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-4943-733X

Funding

X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Sean McSweeney · 2019 to 2026
$38.6M
Discovery of cGAS-like signaling enzymes in innate immunity and diseaseDP2GM146250 · NIGMS · DANA-FARBER CANCER INST · PI KRANZUSCH, PHILIP J · 2021 to 2024
$2.5M
NIGMS NIH HHS DP2 GM146250NIGMS NIH HHS P30 GM133893
6 · The paper itself

Abstract

QueC proteins are nucleoside biosynthesis enzymes required for production of the 7-deazaguanine derivative queuosine. Recently, QueC-family proteins were also shown to catalyze a deazaguanylation protein-nucleobase conjugation reaction in type IV CBASS bacterial anti-phage defense. Here we determine the structural basis of QueC-family protein function in a distinct bacterial immunity system named qatABCD. We demonstrate that the QueC-family protein QatC forms a specific complex with the immunity protein QatB and that this complex is minimally required for qatABCD defense. Crystal structures of the QatBC complex enable direct comparison of qatABCD and type IV CBASS defense and support a shared role for QueC-family proteins in targeting protein substrates for N-terminal modification. We show that the QatB unstructured N-terminus and N-terminal glycine motif are essential for qatABCD defense

Identifiers

PMID40950076
PMCPMC12424860

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.