Evidence map›Paper›PMID 11679764›Full record

ArticleActa crystallographica. Section D, Biological crystallography2001

Streptococcus pneumonia YlxR at 1.35 A shows a putative new fold.

J Osipiuk, P Górnicki, L Maj, I Dementieva, R Laskowski, A Joachimiak

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

18 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Frontiers in microbiology · 2020
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  13. The structural role of the zinc ion can be dispensable in prokaryotic zinc-finger domains.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  14. Article
  15. Automation of protein purification for structural genomics.Journal of structural and functional genomics · 2004
    Article
  16. Article
  17. Article
  18. Review
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

6 authors at 3 institutions in 2 countries.

J OsipiukArgonne National Laboratory, Structural Biology Center, Biosciences Division, IL 60439, USA.
P Górnicki
L Maj
I Dementieva
R Laskowski
A Joachimiak
Argonne National Laboratory · USBirkbeck, University of London · GBUniversity of Chicago · US

Funding

THE MIDWEST CENTER FOR STRUCTURAL GENOMICSP50GM062414 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ JOACHIMIAK · 2000 to 2004
$33.2M
NIGMS NIH HHS GM62414-01NIGMS NIH HHS P50 GM062414
6 · The paper itself

Abstract

The structure of the YlxR protein of unknown function from Streptococcus pneumonia was determined to 1.35 A. YlxR is expressed from the nusA/infB operon in bacteria and belongs to a small protein family (COG2740) that shares a conserved sequence motif GRGA(Y/W). The family shows no significant amino-acid sequence similarity with other proteins. Three-wavelength diffraction MAD data were collected to 1.7 A from orthorhombic crystals using synchrotron radiation and the structure was determined using a semi-automated approach. The YlxR structure resembles a two-layer alpha/beta sandwich with the overall shape of a cylinder and shows no structural homology to proteins of known structure. Structural analysis revealed that the YlxR structure represents a new protein fold that belongs to the alpha-beta plait superfamily. The distribution of the electrostatic surface potential shows a large positively charged patch on one side of the protein, a feature often found in nucleic acid-binding proteins. Three sulfate ions bind to this positively charged surface. Analysis of potential binding sites uncovered several substantial clefts, with the largest spanning 3/4 of the protein. A similar distribution of binding sites and a large sharply bent cleft are observed in RNA-binding proteins that are unrelated in sequence and structure. It is proposed that YlxR is an RNA-binding protein.

Indexed as

RNA-Binding ProteinsAmino Acid SequenceBacterial ProteinsCrystallizationCrystallography, X-RayModels, MolecularMolecular Sequence DataProtein ConformationSequence Homology, Amino AcidStreptococcus pneumoniaeBacterial ProteinsRNA-Binding ProteinsYlxR protein, Streptococcus pneumonia

Identifiers

PMID11679764
PMCPMC2792016
OpenAlexW2120399146

What OpenQuestion holds

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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.