Evidence map›Paper›PMID 14696184›Full record

ArticleProteins2004

Novel protein and Mg2+ configurations in the Mg2+GDP complex of the SRP GTPase ffh.

Pamela J Focia, Hena Alam, Thanh Lu, Ursula D Ramirez, Douglas M Freymann

Open access · bronzeAbstract read
In one paragraph

Article in Proteins, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 21% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Nucleotide-binding flexibility in ultrahigh-resolution structures of the SRP GTPase Ffh.Acta crystallographica. Section D, Biological crystallography · 2008
    Article
  7. Article
  8. Article
  9. Article
  10. Analysis of protein hydration in ultrahigh-resolution structures of the SRP GTPase Ffh.Acta crystallographica. Section D, Biological crystallography · 2006
    Article
  11. 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

5 authors at 1 institution in 1 country.

Pamela J FociaDepartment of Molecular Pharmacology & Biological Chemistry, Northwestern University Medical School, 303 E. Chicago Avenue, Chicago, Illinois 60611, USA.
Hena Alam
Thanh Lu
Ursula D Ramirez
Douglas M Freymann
Northwestern University · US

Funding

VERY HIGH RESOLUTION STRUCTURES OF THE FFH GTPASER01GM058500 · NIGMS · NORTHWESTERN UNIVERSITY · PI FREYMANN, DOUGLAS M. · 1999 to 2005
$1.5M
NIGMS NIH HHS GM58500NIGMS NIH HHS R01 GM058500
6 · The paper itself

Abstract

Ffh is the signal sequence recognition and targeting subunit of the prokaryotic signal recognition particle (SRP). Previous structural studies of the NG GTPase domain of Ffh demonstrated magnesium-dependent and magnesium-independent binding conformations for GDP and GMPPNP that are believed to reflect novel mechanisms for exchange and activation in this member of the GTPase superfamily. The current study of the NG GTPase bound to Mg(2+)GDP reveals two new binding conformations-in the first the magnesium interactions are similar to those seen previously, however, the protein undergoes a conformational change that brings a conserved aspartate into its second coordination sphere. In the second, the protein conformation is similar to that seen previously, but the magnesium coordination sphere is disrupted so that only five oxygen ligands are present. The loss of the coordinating water molecule, at the position that would be occupied by the oxygen of the gamma-phosphate of GTP, is consistent with that position being privileged for exchange during phosphate release. The available structures of the GDP-bound protein provide a series of structural snapshots that illuminate steps along the pathway of GDP release following GTP hydrolysis.

Indexed as

Amino Acid MotifsApoproteinsBacterial ProteinsBinding SitesCrystallography, X-RayGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateGuanylyl ImidodiphosphateHydrolysisLigandsMagnesiumModels, MolecularOxygenProtein ConformationSignal Recognition ParticleApoproteinsBacterial ProteinsGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateGuanylyl ImidodiphosphateLigandsMagnesiumOxygenSignal Recognition Particle

Identifiers

PMID14696184
PMCPMC3540803
OpenAlexW2167702721

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.