Evidence map›Paper›PMID 12235380›Full record

ArticleNucleic acids research2002

High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI.

Erik Werner, Wolfgang Wende, Alfred Pingoud, Udo Heinemann

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Cisplatin protects mice from challenge ofEmerging microbes & infections · 2019
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  4. Article
  5. Article
  6. Crystallization and preliminary X-ray diffraction analysis on the homing endonuclease I-Dmo-I in complex with its target DNA.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007
    Article
  7. NMR structure of a KlbA intein precursor from Methanococcus jannaschii.Protein science : a publication of the Protein Society · 2007
    Article
  8. Article
  9. Article
  10. Article
  11. Evolution of the MAT locus and its Ho endonuclease in yeast species.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  12. 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 1 institution in 1 country.

Erik WernerCrystallography Group, Max Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13092 Berlin, Germany.
Wolfgang Wende
Alfred Pingoud
Udo Heinemann
Max Delbrück Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The homing endonuclease PI-SceI from Saccharo myces cerevisiae consists of two domains. The protein splicing domain I catalyzes the excision of the mature endonuclease (intein) from a precursor protein and the religation of the flanking amino acid sequences (exteins) to a functional protein. Furthermore, domain I is involved in binding and recognition of the specific DNA substrate. Domain II of PI-SceI, the endonuclease domain, which is structurally homologous to other homing endonucleases from the LAGLIDADG family, harbors the endonucleolytic center of PI-SceI, which in vivo initiates the homing process by introducing a double-strand cut in the approximately 35 bp recognition sequence. At 1.35 A resolution, the crystal structure of PI-SceI domain I provides a detailed view of the part of the protein that is responsible for tight and specific DNA binding. A geometry-based docking of the 75 degrees bent recognition sequence to the full-length protein implies a conformational change or hinge movement of a subdomain of domain I, the tongs part, that is predicted to reach into the major groove near base pairs +16 to +18.

Indexed as

Proton-Translocating ATPasesSaccharomyces cerevisiae ProteinsBinding SitesCrystallography, X-RayEndodeoxyribonucleasesFungal ProteinsModels, MolecularProtein ConformationProtein SplicingProtein Structure, TertiarySaccharomyces cerevisiaeEndodeoxyribonucleasesFungal ProteinsProton-Translocating ATPasesSaccharomyces cerevisiae ProteinsVMA1 protein, S cerevisiae

Identifiers

PMID12235380
PMCPMC137108
OpenAlexW2068457771

What OpenQuestion holds

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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.