Evidence map›Paper›PMID 20122942›Full record

ArticleJournal of molecular biology2010

Crystal structure of the first eubacterial Mre11 nuclease reveals novel features that may discriminate substrates during DNA repair.

Debanu Das, Davide Moiani, Herbert L Axelrod, Mitchell D Miller, Daniel McMullan, Kevin K Jin, Polat Abdubek, Tamara Astakhova, Prasad Burra, Dennis Carlton and 37 more

Abstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Modes of action of the archaeal Mre11/Rad50 DNA-repair complex revealed by fast-scan atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Structural basis of homologous recombination.Cellular and molecular life sciences : CMLS · 2020
    Review
  6. Review
  7. Review
  8. Article
  9. Eukaryotic resectosomes: A single-molecule perspective.Progress in biophysics and molecular biology · 2017
    Review
  10. Article
  11. A network of allosterically coupled residues in the bacteriophage T4 Mre11-Rad50 complex.Protein science : a publication of the Protein Society · 2016
    Article
  12. Article
  13. Structure of the catalytic domain of Mre11 from Chaetomium thermophilum.Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. 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

47 authors at 7 institutions in 2 countries.

Debanu DasJoint Center for Structural Genomics, Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
Davide Moiani
Herbert L Axelrod
Mitchell D Miller
Daniel McMullan
Kevin K Jin
Polat Abdubek
Tamara Astakhova
Prasad Burra
Dennis Carlton
Hsiu-Ju Chiu
Thomas Clayton
Marc C Deller
Lian Duan
Dustin Ernst
Julie Feuerhelm
Joanna C Grant
Anna Grzechnik
Slawomir K Grzechnik
Gye Won Han
Lukasz Jaroszewski
Heath E Klock
Mark W Knuth
Piotr Kozbial
S Sri Krishna
Abhinav Kumar
David Marciano
Andrew T Morse
Edward Nigoghossian
Linda Okach
Jessica Paulsen
Ron Reyes
Christopher L Rife
Natasha Sefcovic
Henry J Tien
Christine B Trame
Henry van den Bedem
Dana Weekes
Qingping Xu
Keith O Hodgson
John Wooley
Marc-André Elsliger
Ashley M Deacon
Adam Godzik
Scott A Lesley
John A Tainer
Ian A Wilson
Stanford University · USScripps Research Institute · USNovartis (Switzerland) · CHUniversity of California, San Diego · USDiscovery Institute · USSanford Burnham Prebys Medical Discovery Institute · USSLAC National Accelerator Laboratory · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Technology Evaluation CoreU54GM074898 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI STEVENS, RAYMOND C · 2005 to 2009
$50.6M
JOINT CENTER FOR STRUCTURAL GENOMICSP50GM062411 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI WILSON, IAN A · 2000 to 2004
$32.9M
Mre11/Rad50 Structural Biology for DNA Damage ResponsesR01CA117638 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI RUSSELL, PAUL, TAINER, JOHN A. · 2005 to 2019
$5.6M
NCI NIH HHS CA092584NCI NIH HHS CA117638NCI NIH HHS P01 CA092584NCI NIH HHS R01 CA117638NIGMS NIH HHS P50 GM062411NIGMS NIH HHS P50 GM62411NIGMS NIH HHS U54 GM074898
6 · The paper itself

Abstract

Mre11 nuclease plays a central role in the repair of cytotoxic and mutagenic DNA double-strand breaks. As X-ray structural information has been available only for the Pyrococcus furiosus enzyme (PfMre11), the conserved and variable features of this nuclease across the domains of life have not been experimentally defined. Our crystal structure and biochemical studies demonstrate that TM1635 from Thermotoga maritima, originally annotated as a putative nuclease, is an Mre11 endo/exonuclease (TmMre11) and the first such structure from eubacteria. TmMre11 and PfMre11 display similar overall structures, despite sequence identity in the twilight zone of only approximately 20%. However, they differ substantially in their DNA-specificity domains and in their dimeric organization. Residues in the nuclease domain are highly conserved, but those in the DNA-specificity domain are not. The structural differences likely affect how Mre11 from different organisms recognize and interact with single-stranded DNA, double-stranded DNA and DNA hairpin structures during DNA repair. The TmMre11 nuclease active site has no bound metal ions, but is conserved in sequence and structure with the exception of a histidine that is important in PfMre11 nuclease activity. Nevertheless, biochemical characterization confirms that TmMre11 possesses both endonuclease and exonuclease activities on single-stranded and double-stranded DNA substrates, respectively.

Indexed as

DNA RepairAmino Acid SequenceBacterial ProteinsCrystallography, X-RayDNADNA, Single-StrandedEndodeoxyribonucleasesExodeoxyribonucleasesModels, ChemicalMolecular Sequence DataProtein ConformationSequence Homology, Amino AcidThermotoga maritimaBacterial ProteinsDNADNA, Single-StrandedEndodeoxyribonucleasesExodeoxyribonucleases

Identifiers

PMID20122942
PMCPMC2839085
OpenAlexW2073954040

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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.