Evidence map›Paper›PMID 18978942›Full record

ArticlePloS one2008

Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane.

Pascal F Egea, Hiro Tsuruta, Gladys P de Leon, Johanna Napetschnig, Peter Walter, Robert M Stroud

Open access · goldAbstract readComparative Study
In one paragraph

Article in PloS one, 2008. 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
1.9field-weighted citation impact, top 14% 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, 23 citations in OpenAlex.

  1. Review
  2. Molecular Characterization of Tc964, A Novel Antigenic Protein fromInternational journal of molecular sciences · 2020
    Article
  3. Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018
    Article
  4. Article
  5. Review
  6. Article
  7. Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  8. Review
  9. Article
  10. Protein transport across and into cell membranes in bacteria and archaea.Cellular and molecular life sciences : CMLS · 2010
    Review
  11. 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

6 authors at 2 institutions in 1 country.

Pascal F EgeaDepartment of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California, USA. pascal@msg.ucsf.edu
Hiro Tsuruta
Gladys P de Leon
Johanna Napetschnig
Peter Walter
Robert M Stroud
University of California, San Francisco · USStanford University · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
SIGNAL SEQUENCE RECOGNITION AND PROTEIN TARGETINGR01GM060641 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2000 to 2007
$2.4M
NCRR NIH HHS 5 P41 RR001209NCRR NIH HHS P41 RR001209NIGMS NIH HHS GM60641NIGMS NIH HHS R01 GM060641
6 · The paper itself

Abstract

In all organisms, a ribonucleoprotein called the signal recognition particle (SRP) and its receptor (SR) target nascent proteins from the ribosome to the translocon for secretion or membrane insertion. We present the first X-ray structures of an archeal FtsY, the receptor from the hyper-thermophile Pyrococcus furiosus (Pfu), in its free and GDP*magnesium-bound forms. The highly charged N-terminal domain of Pfu-FtsY is distinguished by a long N-terminal helix. The basic charges on the surface of this helix are likely to regulate interactions at the membrane. A peripheral GDP bound near a regulatory motif could indicate a site of interaction between the receptor and ribosomal or SRP RNAs. Small angle X-ray scattering and analytical ultracentrifugation indicate that the crystal structure of Pfu-FtsY correlates well with the average conformation in solution. Based on previous structures of two sub-complexes, we propose a model of the core of archeal and eukaryotic SRP*SR targeting complexes.

Indexed as

Pyrococcus furiosusAmino Acid SequenceArabidopsis ProteinsCell MembraneChloroplast ProteinsCrystallography, X-RayDNA-Directed DNA PolymeraseGuanosine DiphosphateMembrane ProteinsModels, MolecularProtein BindingProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryProtein TransportReceptors, Cytoplasmic and NuclearArabidopsis ProteinsChloroplast ProteinscpFtsY protein, ArabidopsisDNA-Directed DNA PolymeraseGuanosine DiphosphateMembrane ProteinsPfu DNA polymeraseReceptors, Cytoplasmic and NuclearReceptors, Peptidesignal peptide receptor

Identifiers

PMID18978942
PMCPMC2572998
OpenAlexW2006163880

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.