Evidence map›Paper›PMID 30385633›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Deciphering the structure of the condensin protein complex.

Dana Krepel, Ryan R Cheng, Michele Di Pierro, José N Onuchic

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. 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
1.3field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  4. Motorized chain models of the ideal chromosome.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  13. Braiding topology and the energy landscape of chromosome organization proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

4 authors at 2 institutions in 1 country.

Dana KrepelCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005; danakrezus@rice.edu jonuchic@rice.edu.
Ryan R ChengCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005.
Michele Di PierroCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005.
José N OnuchicCenter for Theoretical Biological Physics, Rice University, Houston, TX 77005; danakrezus@rice.edu jonuchic@rice.edu.
Center for Theoretical Biological Physics · USRice University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein assemblies consisting of structural maintenance of chromosomes (SMC) and kleisin subunits are essential for the process of chromosome segregation across all domains of life. Prokaryotic condensin belonging to this class of protein complexes is composed of a homodimer of SMC that associates with a kleisin protein subunit called ScpA. While limited structural data exist for the proteins that comprise the (SMC)-kleisin complex, the complete structure of the entire complex remains unknown. Using an integrative approach combining both crystallographic data and coevolutionary information, we predict an atomic-scale structure of the whole condensin complex, which our results indicate being composed of a single ring. Coupling coevolutionary information with molecular-dynamics simulations, we study the interaction surfaces between the subunits and examine the plausibility of alternative stoichiometries of the complex. Our analysis also reveals several additional configurational states of the condensin hinge domain and the SMC-kleisin interaction domains, which are likely involved with the functional opening and closing of the condensin ring. This study provides the foundation for future investigations of the structure-function relationship of the various SMC-kleisin protein complexes at atomic resolution.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceBacterial ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneChromosomesChromosome SegregationDatabases, ProteinDNA-Binding ProteinsMultiprotein ComplexesNuclear ProteinsProtein DomainsStructure-Activity RelationshipAdenosine TriphosphatasesBacterial ProteinsCell Cycle ProteinsChromosomal Proteins, Non-Histonecondensin complexesDNA-Binding ProteinsMultiprotein ComplexesNuclear ProteinsScpA protein, Bacillus subtilisSMC protein, Bacteriabacterial condensincoevolutionary informationdirect coupling analysisDNA translocationSMC–kleisin complexes

Identifiers

PMID30385633
PMCPMC6255159
OpenAlexW2899461463

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.