Evidence map›Paper›PMID 42129268›Full record

ArticleNature communications2026

Structural investigation of QatB and QatC proteins in QatABCD anti-phage defense.

Hyejin Oh, Euiyoung Bae

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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

2 authors.

Hyejin OhDepartment of Agricultural Biotechnology, Seoul National University, Seoul, Korea.
Euiyoung BaeDepartment of Agricultural Biotechnology, Seoul National University, Seoul, Korea. bae@snu.ac.kr.ORCID http://orcid.org/0000-0001-7865-0167

Funding

National Research Foundation of Korea (NRF) NRF-2022R1A2C1009804National Research Foundation of Korea (NRF) RS-2023-00207820National Research Foundation of Korea (NRF) RS-2024-00408183
6 · The paper itself

Abstract

QatABCD is a widespread anti-phage defense system in prokaryotes comprising four protein components. QatC, a signature component, is homologous to QueC, an enzyme involved in nucleobase modification during queuosine biosynthesis. QatA and QatD are predicted to function as an ATPase and a nuclease, respectively, while QatB lacks identifiable sequence motifs. Here, we report the structural and functional characterization of QatB and QatC. We determine the structure of QatC bound to the ATP analog AMPPNP and perform structure-guided functional assays. We further find that QatB and QatC form a stable heterodimer and solve the structure of the QatB-QatC complex. In addition to determining the structure of QatB, structural analysis suggests that it may serve as a substrate of QatC, implicating a potential regulatory mechanism. These findings provide structural and functional insights into QatB and QatC, laying a foundation for understanding the molecular mechanism of the QatABCD system in phage defense.

Indexed as

BacteriophagesEscherichia coli ProteinsAdenosine TriphosphatasesAdenosine TriphosphateCrystallography, X-RayEscherichia coliModels, MolecularAdenosine TriphosphatasesAdenosine TriphosphateEscherichia coli Proteins

Identifiers

PMID42129268
PMCPMC13376578

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.