Evidence map›Paper›PMID 18400177›Full record

ArticleStructure (London, England : 1993)2008

Structures of the rare-cutting restriction endonuclease NotI reveal a unique metal binding fold involved in DNA binding.

Abigail R Lambert, Django Sussman, Betty Shen, Robert Maunus, Jay Nix, James Samuelson, Shuang-Yong Xu, Barry L Stoddard

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  5. Analysis of the HindIII-catalyzed reaction by time-resolved crystallography.Acta crystallographica. Section D, Biological crystallography · 2015
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  6. Review
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  15. DNA-mediated charge transport in redox sensing and signaling.Journal of the American Chemical Society · 2010
    Article
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  17. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Abigail R LambertGraduate Program in Biomolecular Structure and Design, University of Washington, Seattle, WA 98195, USA.
Django Sussman
Betty Shen
Robert Maunus
Jay Nix
James Samuelson
Shuang-Yong Xu
Barry L Stoddard
Fred Hutch Cancer Center · USUniversity of Washington · USLawrence Berkeley National Laboratory · US

Funding

TRAINING IN MOLECULAR AND CELLULAR BIOLOGYT32GM007270 · NIGMS · UNIVERSITY OF WASHINGTON · PI RAIBLE, DAVID W · 1985 to 2020
$21.0M
XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 1985 to 2011
$17.6M
Structure, function &engineering of nuclease catalystsR01GM049857 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI STODDARD, BARRY L. · 1994 to 2014
$4.2M
NCRR NIH HHS P41 RR001081NCRR NIH HHS P41 RR-01081NIGMS NIH HHS R01 GM049857NIGMS NIH HHS R01 GM49857NIGMS NIH HHS T32 GM007270NIGMS NIH HHS T32 GM07270
6 · The paper itself

Abstract

The structure of the rare-cutting restriction endonuclease NotI, which recognizes the 8 bp target 5'-GCGGCCGC-3', has been solved with and without bound DNA. Because of its specificity (recognizing a site that occurs once per 65 kb), NotI is used to generate large genomic fragments and to map DNA methylation status. NotI contains a unique metal binding fold, found in a variety of putative endonucleases, occupied by an iron atom coordinated within a tetrahedral Cys4 motif. This domain positions nearby protein elements for DNA recognition, and serves a structural role. While recognition of the central six base pairs of the target is accomplished via a saturated hydrogen bond network typical of restriction enzymes, the most peripheral base pairs are engaged in a single direct contact in the major groove, reflecting reduced pressure to recognize those positions. NotI may represent an evolutionary intermediate between mobile endonucleases (which recognize longer target sites) and canonical restriction endonucleases.

Indexed as

Models, MolecularAmino Acid SequenceBinding SitesCrystallography, X-RayDeoxyribonucleases, Type II Site-SpecificDNAIronMolecular Sequence DataProtein BindingProtein FoldingProtein Structure, TertiarySequence Homology, Amino AcidSubstrate SpecificityDeoxyribonucleases, Type II Site-SpecificDNAGCGGCCGC-specific type II deoxyribonucleasesIron

Identifiers

PMID18400177
PMCPMC2390919
OpenAlexW2056703179

What OpenQuestion holds

Textmetadata
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.