Evidence map›Paper›PMID 18424798›Full record

ArticleNucleic acids research2008

Crystal structures of I-SceI complexed to nicked DNA substrates: snapshots of intermediates along the DNA cleavage reaction pathway.

Carmen M Moure, Frederick S Gimble, Florante A Quiocho

Abstract read
In one paragraph

Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Visualizing phosphodiester-bond hydrolysis by an endonuclease.Nature structural & molecular biology · 2015
    Article
  4. Article
  5. Article
  6. Nucleases: diversity of structure, function and mechanism.Quarterly reviews of biophysics · 2011
    Review
  7. Review
  8. Article
  9. Review
  10. Homing endonucleases: from basics to therapeutic applications.Cellular and molecular life sciences : CMLS · 2010
    Review
  11. Generation of a nicking enzyme that stimulates site-specific gene conversion from the I-AniI LAGLIDADG homing endonuclease.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  12. Crystal structure of I-DmoI in complex with its target DNA provides new insights into meganuclease engineering.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  13. 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

3 authors.

Carmen M MoureVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA. mmoure@bcm.tmc.edu
Frederick S Gimble
Florante A Quiocho

Funding

Engineering DNA Endonuclease Reagents for Gene TargetingR01GM070553 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI GIMBLE, FREDERICK SAMUEL · 2004 to 2008
$870k
NIGMS NIH HHS GM 070553NIGMS NIH HHS R01 GM070553
6 · The paper itself

Abstract

I-SceI is a homing endonuclease that specifically cleaves an 18-bp double-stranded DNA. I-SceI exhibits a strong preference for cleaving the bottom strand DNA. The published structure of I-SceI bound to an uncleaved DNA substrate provided a mechanism for bottom strand cleavage but not for top strand cleavage. To more fully elucidate the I-SceI catalytic mechanism, we determined the X-ray structures of I-SceI in complex with DNA substrates that are nicked in either the top or bottom strands. The structures resemble intermediates along the DNA cleavage reaction. In a structure containing a nick in the top strand, the spatial arrangement of metal ions is similar to that observed in the structure that contains uncleaved DNA, suggesting that cleavage of the bottom strand occurs by a common mechanism regardless of whether this strand is cleaved first or second. In the structure containing a nick in the bottom strand, a new metal binding site is present in the active site that cleaves the top strand. This new metal and a candidate nucleophilic water molecule are correctly positioned to cleave the top strand following bottom strand cleavage, providing a plausible mechanism for top strand cleavage.

Indexed as

Models, MolecularBinding SitesCalciumCatalysisCatalytic DomainCrystallography, X-RayDeoxyribonucleases, Type II Site-SpecificDNAProtein ConformationSaccharomyces cerevisiae ProteinsCalciumDeoxyribonucleases, Type II Site-SpecificDNASaccharomyces cerevisiae ProteinsSCEI protein, S cerevisiae

Identifiers

PMID18424798
PMCPMC2425494

What OpenQuestion holds

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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.