Evidence map›Paper›PMID 18452512›Full record

ArticleMolecular microbiology2008

Localization and nucleotide specificity of Blastocystis succinyl-CoA synthetase.

Karleigh Hamblin, Daron M Standley, Matthew B Rogers, Alexandra Stechmann, Andrew J Roger, Robin Maytum, Mark van der Giezen

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Second distinct conformation of the phosphohistidine loop in succinyl-CoA synthetase.Acta crystallographica. Section D, Structural biology · 2021
    Article
  2. Article
  3. The Human Gut ColonizerFrontiers in cellular and infection microbiology · 2018
    Article
  4. Article
  5. Article
  6. Biochemistry and evolution of anaerobic energy metabolism in eukaryotes.Microbiology and molecular biology reviews : MMBR · 2012
    Review
  7. Article
  8. Diversity and reductive evolution of mitochondria among microbial eukaryotes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2010
    Review
  9. Article
  10. 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

7 authors at 3 institutions in 3 countries.

Karleigh HamblinSchool of Biological and Chemical Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, UK.
Daron M Standley
Matthew B Rogers
Alexandra Stechmann
Andrew J Roger
Robin Maytum
Mark van der Giezen
Queen Mary University of London · GBDalhousie University · CAJapan Science and Technology Agency · JP

Funding

Wellcome Trust 078566Wellcome Trust 078566/A/05/Z
6 · The paper itself

Abstract

The anaerobic lifestyle of the intestinal parasite Blastocystis raises questions about the biochemistry and function of its mitochondria-like organelles. We have characterized the Blastocystis succinyl-CoA synthetase (SCS), a tricarboxylic acid cycle enzyme that conserves energy by substrate-level phosphorylation. We show that SCS localizes to the enigmatic Blastocystis organelles, indicating that these organelles might play a similar role in energy metabolism as classic mitochondria. Although analysis of residues inside the nucleotide-binding site suggests that Blastocystis SCS is GTP-specific, we demonstrate that it is ATP-specific. Homology modelling, followed by flexible docking and molecular dynamics simulations, indicates that while both ATP and GTP fit into the Blastocystis SCS active site, GTP is destabilized by electrostatic dipole interactions with Lys 42 and Lys 110, the side-chains of which lie outside the nucleotide-binding cavity. It has been proposed that residues in direct contact with the substrate determine nucleotide specificity in SCS. However, our results indicate that, in Blastocystis, an electrostatic gatekeeper controls which ligands can enter the binding site.

Indexed as

AnimalsBase SequenceBlastocystisBlastocystis InfectionsCytoplasmic StructuresHumansKineticsModels, MolecularMolecular Sequence DataPhylogenyProtein SubunitsProtozoan ProteinsPurine NucleotidesSequence AlignmentSubstrate SpecificitySuccinate-CoA LigasesProtein SubunitsProtozoan ProteinsPurine NucleotidesSuccinate-CoA Ligases

Identifiers

PMID18452512
PMCPMC2440562
OpenAlexW2142522424

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.