Evidence map›Paper›PMID 20800503›Full record

ArticleStructure (London, England : 1993)2010

Folding, DNA recognition, and function of GIY-YIG endonucleases: crystal structures of R.Eco29kI.

Amanda Nga-Sze Mak, Abigail R Lambert, Barry L Stoddard

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

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  14. Human ANKLE1 Is a Nuclease Specific for Branched DNA.Journal of molecular biology · 2020
    Article
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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.

Amanda Nga-Sze MakDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA.
Abigail R Lambert
Barry L Stoddard

Funding

Structure, function &engineering of nuclease catalystsR01GM049857 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI STODDARD, BARRY L. · 1994 to 2014
$4.2M
Structural and Biophysical Characterization of Engineered Homing Endonucleases (CRL1CA133833 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI STODDARD, BARRY L. · 2007 to 2011
$2.1M
NCI NIH HHS RL1 CA133833NIGMS NIH HHS R01 GM049857NIGMS NIH HHS R01 GM49857
6 · The paper itself

Abstract

The GIY-YIG endonuclease family comprises hundreds of diverse proteins and a multitude of functions; none have been visualized bound to DNA. The structure of the GIY-YIG restriction endonuclease R.Eco29kI has been solved both alone and bound to its target site. The protein displays a domain-swapped homodimeric structure with several extended surface loops encircling the DNA. Only three side chains from each protein subunit contact DNA bases, two directly and one via a bridging solvent molecule. Both tyrosine residues within the GIY-YIG motif are positioned in the catalytic center near a putative nucleophilic water; the remainder of the active site resembles the HNH endonuclease family. The structure illustrates how the GIY-YIG scaffold has been adapted for the highly specific recognition of a DNA restriction site, in contrast to nonspecific DNA cleavage by GIY-YIG domains in homing endonucleases or structure-specific cleavage by DNA repair enzymes such as UvrC.

Indexed as

Protein FoldingProtein Structure, TertiaryAmino Acid SequenceBase SequenceBinding SitesCrystallizationCrystallography, X-RayDeoxyribonucleases, Type II Site-SpecificDNAModels, MolecularMolecular Sequence DataMutation, MissenseProtein BindingProtein MultimerizationSequence Homology, Amino AcidCCGCGG-specific type II deoxyribonucleasesDeoxyribonucleases, Type II Site-SpecificDNA

Identifiers

PMID20800503
PMCPMC2955809

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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.