Evidence map›Paper›PMID 33058314›Full record

ArticleProtein science : a publication of the Protein Society2020

Chlamydia trachomatis glyceraldehyde 3-phosphate dehydrogenase: Enzyme kinetics, high-resolution crystal structure, and plasminogen binding.

Norbert Schormann, Juan Campos, Rachael Motamed, Katherine L Hayden, Joseph R Gould, Todd J Green, Olga Senkovich, Surajit Banerjee, Glen C Ulett, Debasish Chattopadhyay

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

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface ofInternational journal of molecular sciences · 2024
    Article
  3. The role of tryptophan inFrontiers in cellular and infection microbiology · 2022
    Review
  4. Article
  5. 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

10 authors at 5 institutions in 2 countries.

Norbert SchormannDepartment of Biochemistry, University of Alabama at Birmingham, Birmingham, Alabama, USA.
Juan CamposDepartment of Chemistry and Physics, Birmingham-Southern College, Birmingham, Alabama, USA.
Rachael MotamedDepartment of Chemistry and Physics, Birmingham-Southern College, Birmingham, Alabama, USA.
Katherine L HaydenDepartment of Chemistry and Physics, Birmingham-Southern College, Birmingham, Alabama, USA.
Joseph R GouldDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA.
Todd J GreenDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA.
Olga SenkovichDepartment of Biochemistry and Molecular Genetics, Midwestern University, Glendale, Arizona, USA.
Surajit BanerjeeNortheastern Collaborative Access Team and Department of Chemistry and Chemical Biology, Cornell University, Argonne, Illinois, USA.
Glen C UlettSchool of Medical Sciences, and Menzies Health Institute Queensland, Griffith University, Parklands, Australia.
Debasish ChattopadhyayDepartment of Medicine, University of Alabama at Birmingham, Birmingham, Alabama, USA.ORCID 0000-0001-5262-9140
University of Alabama at Birmingham · USBirmingham–Southern College · USArgonne National Laboratory · USGriffith University · AUMidwestern University · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P30 GM124165NIH HHS P30 GM124165
6 · The paper itself

Abstract

Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an evolutionarily conserved essential enzyme in the glycolytic pathway. GAPDH is also involved in a wide spectrum of non-catalytic cellular 'moonlighting' functions. Bacterial surface-associated GAPDHs engage in many host interactions that aid in colonization, pathogenesis, and virulence. We have structurally and functionally characterized the recombinant GAPDH of the obligate intracellular bacteria Chlamydia trachomatis, the leading cause of sexually transmitted bacterial and ocular infections. Contrary to earlier speculations, recent data confirm the presence of glucose-catabolizing enzymes including GAPDH in both stages of the biphasic life cycle of the bacterium. The high-resolution crystal structure described here provides a close-up view of the enzyme's active site and surface topology and reveals two chemically modified cysteine residues. Moreover, we show for the first time that purified C. trachomatis GAPDH binds to human plasminogen and plasmin. Based on the versatility of GAPDH's functions, data presented here emphasize the need for investigating the Chlamydiae GAPDH's involvement in biological functions beyond energy metabolism.

Indexed as

Models, MolecularBacterial ProteinsChlamydia trachomatisCrystallography, X-RayGlyceraldehyde-3-Phosphate DehydrogenasesPlasminogenProtein BindingBacterial ProteinsGlyceraldehyde-3-Phosphate DehydrogenasesPlasminogenChlamydiacrystal structureenzyme kineticsGAPDHglycolysisplasmin bindingplasminogen bindingprotein-protein interactionreactive cysteineSTD/STI

Identifiers

PMID33058314
PMCPMC7679969
OpenAlexW3092932157

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.