Evidence map›Paper›PMID 25286935›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface.

Chapelle A Ayres, Norbert Schormann, Olga Senkovich, Alexandra Fry, Surajit Banerjee, Glen C Ulett, Debasish Chattopadhyay

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 24% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. International journal of molecular sciences · 2020
    Article
  4. High-resolution crystal structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  5. Article
  6. 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 2 countries.

Chapelle A AyresScience and Technology Honors Program, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Norbert SchormannCenter for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Olga SenkovichDepartment of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Alexandra FryScience and Technology Honors Program, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Surajit BanerjeeNortheastern Collaborative Access Team and Department of Chemistry and Chemical Biology, Cornell University, Argonne, IL 60439, USA.
Glen C UlettSchool of Medical Science and Griffith Health Institute, Griffith University, QLD 4222, Australia.
Debasish ChattopadhyayCenter for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
University of Alabama at Birmingham · USCornell University · USGriffith University · AU

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a conserved cytosolic enzyme, which plays a key role in glycolysis. GAPDH catalyzes the oxidative phosphorylation of D-glyceraldehyde 3-phosphate using NAD or NADP as a cofactor. In addition, GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate. Here, the crystal structure of GBS GAPDH from Streptococcus agalactiae in complex with NAD is reported at 2.46 Å resolution. Although the overall structure of GBS GAPDH is very similar to those of other GAPDHs, the crystal structure reveals a significant difference in the area spanning residues 294-307, which appears to be more acidic. The amino-acid sequence of this region of GBS GAPDH is also distinct compared with other GAPDHs. This region therefore may be of interest as an immunogen for vaccine development.

Indexed as

Amino Acid SequenceBacterial ProteinsCatalytic DomainConserved SequenceCrystallography, X-RayGlyceraldehyde-3-Phosphate DehydrogenasesModels, MolecularMolecular Sequence DataNADProtein BindingProtein Structure, QuaternaryStreptococcus agalactiaeStructural Homology, ProteinSurface PropertiesBacterial ProteinsGlyceraldehyde-3-Phosphate DehydrogenasesNADglyceraldehyde 3-phosphate dehydrogenaseStreptococcus agalactiae

Identifiers

PMID25286935
PMCPMC4188075
OpenAlexW2042397974

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.