Evidence map›Paper›PMID 27399259›Full record

ArticleNature structural & molecular biology2016

Structure of chromatin remodeler Swi2/Snf2 in the resting state.

Xian Xia, Xiaoyu Liu, Tong Li, Xianyang Fang, Zhucheng Chen

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

42 citing papers in PubMed, 64 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Xian XiaMOE Key Laboratory of Protein Science, Tsinghua University, Beijing, China.
Xiaoyu LiuMOE Key Laboratory of Protein Science, Tsinghua University, Beijing, China.
Tong LiSchool of Life Science, Tsinghua University, Beijing, China.
Xianyang FangSchool of Life Science, Tsinghua University, Beijing, China.
Zhucheng ChenMOE Key Laboratory of Protein Science, Tsinghua University, Beijing, China.
Tsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SWI2/SNF2 family proteins regulate a myriad of nucleic acid transactions by sliding, removing and reconstructing nucleosomes in eukaryotic cells. They contain two RecA-like core domains, which couple ATP hydrolysis and DNA translocation to chromatin remodeling. Here we report the crystal structure of Snf2 from the yeast Myceliophthora thermophila. The data show the two RecA-like core domains of Snf2 stacking together and twisting their ATP-binding motifs away from each other, thus explaining the inactivity of the protein in the ground state. We identified several DNA-binding elements, which are fully exposed to solvent, thus suggesting that the protein is poised for its incoming substrate. The catalytic core of Snf2 showed a high chromatin-remodeling activity, which was suppressed by the N-terminal HSA domain. Our findings reveal that the catalytic core of Snf2 is a competent remodeling machine, which rests in an inactive conformation and requires a large conformational change upon activation.

Indexed as

Adenosine TriphosphatasesAscomycotaCatalytic DomainCrystallography, X-RayEnzyme ActivationFungal ProteinsHydrophobic and Hydrophilic InteractionsKineticsModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Structure, QuaternaryAdenosine TriphosphatasesFungal Proteins

Identifiers

PMID27399259
OpenAlexW2474148867

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.