Evidence map›Paper›PMID 21565697›Full record

ArticleStructure (London, England : 1993)2011

Structure and activity of a novel archaeal β-CASP protein with N-terminal KH domains.

Ana P G Silva, Maria Chechik, Robert T Byrne, David G Waterman, C Leong Ng, Eleanor J Dodson, Eugene V Koonin, Alfred A Antson, Callum Smits

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

  1. Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Archaeal transcription.Transcription · 2020
    Review
  10. Article
  11. Molecular basis for the interaction between Integrator subunits IntS9 and IntS11 and its functional importance.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. 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

9 authors at 3 institutions in 2 countries.

Ana P G SilvaYork Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, United Kingdom.
Maria Chechik
Robert T Byrne
David G Waterman
C Leong Ng
Eleanor J Dodson
Eugene V Koonin
Alfred A Antson
Callum Smits
University of York · GBMRC Laboratory of Molecular Biology · GBNational Institutes of Health · US

Funding

Finding Protein Sequence Motifs--Methods And ApplicationsZIALM000061 · NLM · NATIONAL LIBRARY OF MEDICINE · PI KOONIN, EUGENE V · 2009 to 2025
$10.6M
Wellcome TrustWellcome Trust 081916
6 · The paper itself

Abstract

MTH1203, a β-CASP metallo-β-lactamase family nuclease from the archaeon Methanothermobacter thermautotrophicus, was identified as a putative nuclease that might contribute to RNA processing. The crystal structure of MTH1203 reveals that, in addition to the metallo-β-lactamase nuclease and the β-CASP domains, it contains two contiguous KH domains that are unique to MTH1203 and its orthologs. RNA-binding experiments indicate that MTH1203 preferentially binds U-rich sequences with a dissociation constant in the micromolar range. In vitro nuclease activity assays demonstrated that MTH1203 is a zinc-dependent nuclease. MTH1203 is also shown to be a dimer and, significantly, this dimerization enhances the nuclease activity. Transcription termination in archaea produces mRNA transcripts with U-rich 3' ends that could be degraded by MTH1203 considering its RNA-binding specificity. We hypothesize that this nuclease degrades mRNAs of proteins targeted for degradation and so regulates archaeal RNA turnover, possibly in concert with the exosome.

Indexed as

Amino Acid SequenceArchaeal ProteinsBase Sequencebeta-LactamasesBinding SitesCloning, MolecularCrystallography, X-RayDimerizationEscherichia coliExonucleasesKineticsMethanobacteriaceaeModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, TertiaryArchaeal Proteinsbeta-LactamasesExonucleasesnuclease betaRecombinant ProteinsRNA-Binding ProteinsZinc

Identifiers

PMID21565697
PMCPMC3095777
OpenAlexW2091114749

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.