Evidence map›Paper›PMID 23999294›Full record

ArticleActa crystallographica. Section D, Biological crystallography2013

Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism.

Stefano Stella, Rafael Molina, Igor Yefimenko, Jesús Prieto, George Silva, Claudia Bertonati, Alexandre Juillerat, Phillippe Duchateau, Guillermo Montoya

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. TALENs-an indispensable tool in the era of CRISPR: a mini review.Journal, genetic engineering & biotechnology · 2021
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  14. BuD, a helix-loop-helix DNA-binding domain for genome modification.Acta crystallographica. Section D, Biological crystallography · 2014
    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

9 authors at 1 institution in 1 country.

Stefano StellaStructural Biology and Biocomputing Programme, Spanish Cancer Research Centre (CNIO), Melchor Fernandez Almagro, 28029 Madrid, Spain.
Rafael Molina
Igor Yefimenko
Jesús Prieto
George Silva
Claudia Bertonati
Alexandre Juillerat
Phillippe Duchateau
Guillermo Montoya
Spanish National Cancer Research Centre · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcription activator-like effectors contain a DNA-binding domain organized in tandem repeats. The repeats include two adjacent residues known as the repeat variable di-residue, which recognize a single base pair, establishing a direct code between the dipeptides and the target DNA. This feature suggests this scaffold as an excellent candidate to generate new protein-DNA specificities for biotechnological applications. Here, the crystal structure of AvrBs3 (residues 152-895, molecular mass 82 kDa) in complex with its target DNA sequence is presented, revealing a new mode of interaction with the initial thymine of the target sequence, together with an analysis of both the binding specificity and the thermodynamic properties of AvrBs3. This study quantifies the affinity and the specificity between AvrBs3 and its target DNA. Moreover, in vitro and in vivo analyses reveal that AvrBs3 does not show a strict nucleotide-binding preference for the nucleotide at the zero position of the DNA, widening the number of possible sequences that could be targeted by this scaffold.

Indexed as

Bacterial ProteinsCrystallizationCrystallography, X-RayDipeptidesDNA, AntisenseDNA, BacterialDNA-Binding ProteinsGene TargetingNucleic Acid HeteroduplexesProtein Interaction MappingTandem Repeat SequencesThermodynamicsThymineTranscription Activator-Like EffectorsTranscriptional ActivationavrBs3-2 protein, Xanthomonas campestrisBacterial ProteinsDipeptidesDNA, AntisenseDNA, BacterialDNA-Binding ProteinsNucleic Acid HeteroduplexesThymineTranscription Activator-Like Effectorsgene targetinggeneticsprotein–DNA interaction

Identifiers

PMID23999294
PMCPMC3760130
OpenAlexW2125135674

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.