ArticleNature communications2019
Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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.
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.
Who cites it
14 citing papers in PubMed, 17 citations in OpenAlex.
- Computational introspection of impact of mutation A90V and A90E in DNA gyrase a of Mycobacterium tuberculosis in developing resistance against Delafloxacin.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Biology of host-dependent restriction-modification in prokaryotes.EcoSal Plus · 2025Review
- PcdA promotes orthogonal division plane selection in Staphylococcus aureus.Nature microbiology · 2024Article
- Article
- Insights into virulence: structure classification of themSystems · 2023Article
- Characterisation of neonatalMicrobial genomics · 2023Article
- Article
- A mobile restriction-modification system provides phage defence and resolves an epigenetic conflict with an antagonistic endonuclease.Nucleic acids research · 2022Article
- AAA+ ATPases: structural insertions under the magnifying glass.Current opinion in structural biology · 2021Review
- Structural asymmetry governs the assembly and GTPase activity of McrBC restriction complexes.Nature communications · 2020Article
- Modified base-binding EVE and DCD domains: striking diversity of genomic contexts in prokaryotes and predicted involvement in a variety of cellular processes.BMC biology · 2020Article
- Biochemical and structural basis for YTH domain of human YTHDC1 binding to methylated adenine in DNA.Nucleic acids research · 2020Article
- The N-terminal domain of Staphylothermus marinus McrB shares structural homology with PUA-like RNA binding proteins.Journal of structural biology · 2020Article
- AAA+ proteins: converging mechanisms, diverging functions.Nature structural & molecular biology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The AAA+ GTPase McrB powers DNA cleavage by the endonuclease McrC. The GTPase itself is activated by McrC. The architecture of the GTPase and nuclease complex, and the mechanism of their activation remained unknown. Here, we report a 3.6 Å structure of a GTPase-active and DNA-binding deficient construct of McrBC. Two hexameric rings of McrB are bridged by McrC dimer. McrC interacts asymmetrically with McrB protomers and inserts a stalk into the pore of the ring, reminiscent of the γ subunit complexed to α
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.