Evidence map›Paper›PMID 26626129›Full record

ArticleMicrobiologyOpen2016

Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm.

Ranjit K Deka, Chad A Brautigam, Wei Z Liu, Diana R Tomchick, Michael V Norgard

Open access · goldAbstract read
In one paragraph

Article in MicrobiologyOpen, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Flavin transferase ApbE: From discovery to applications.The Journal of biological chemistry · 2025
    Review
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  10. Conserved residue His-257 ofThe Journal of biological chemistry · 2019
    Article
  11. Is there a Function for a Sex Pheromone Precursor?Journal of integrative bioinformatics · 2019
    Article
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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.

Ranjit K DekaDepartment of Microbiology, The University of Texas Southwestern Medical Center, Dallas, Texas, 75390.
Chad A BrautigamDepartment of Biophysics, The University of Texas Southwestern Medical Center, Dallas, Texas, 75390.
Wei Z LiuDepartment of Microbiology, The University of Texas Southwestern Medical Center, Dallas, Texas, 75390.
Diana R TomchickDepartment of Biophysics, The University of Texas Southwestern Medical Center, Dallas, Texas, 75390.
Michael V NorgardDepartment of Microbiology, The University of Texas Southwestern Medical Center, Dallas, Texas, 75390.
The University of Texas Southwestern Medical Center · US

Funding

The flavin-centric metabolic lifestyle of Treponema pallidumR01AI056305 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI HENDRIXSON, DAVID R · 2003 to 2024
$9.6M
NIAID NIH HHS 5R01AI056305-12NIAID NIH HHS AI-056305NIAID NIH HHS R01 AI056305
6 · The paper itself

Abstract

We recently reported a flavin-trafficking protein (Ftp) in the syphilis spirochete Treponema pallidum (Ftp_Tp) as the first bacterial metal-dependent FAD pyrophosphatase that hydrolyzes FAD into AMP and FMN in the periplasm. Orthologs of Ftp_Tp in other bacteria (formerly ApbE) appear to lack this hydrolytic activity; rather, they flavinylate the redox subunit, NqrC, via their metal-dependent FMN transferase activity. However, nothing has been known about the nature or mechanism of metal-dependent Ftp catalysis in either Nqr- or Rnf-redox-containing bacteria. In the current study, we identified a bimetal center in the crystal structure of Escherichia coli Ftp (Ftp_Ec) and show via mutagenesis that a single amino acid substitution converts it from an FAD-binding protein to a Mg(2+)-dependent FAD pyrophosphatase (Ftp_Tp-like). Furthermore, in the presence of protein substrates, both types of Ftps are capable of flavinylating periplasmic redox-carrying proteins (e.g., RnfG_Ec) via the metal-dependent covalent attachment of FMN. A high-resolution structure of the Ftp-mediated flavinylated protein of Shewanella oneidensis NqrC identified an essential lysine in phosphoester-threonyl-FMN bond formation in the posttranslationally modified flavoproteins. Together, these discoveries broaden our understanding of the physiological capabilities of the bacterial periplasm, and they also clarify a possible mechanism by which flavoproteins are generated.

Indexed as

Protein Processing, Post-TranslationalAdenosine MonophosphateBacterial ProteinsCrystallography, X-RayEscherichia coliFlavin-Adenine DinucleotideFlavin MononucleotideFlavoproteinsMutagenesis, Site-DirectedOxidation-ReductionPeriplasmProtein TransportPyrophosphatasesShewanellaAdenosine MonophosphateBacterial ProteinsFAD pyrophosphataseFlavin-Adenine DinucleotideFlavin MononucleotideFlavoproteinsPyrophosphatasesFAD pyrophosphataseflavoproteinFMN transferaselipoproteinposttranslational modificationredox protein

Identifiers

PMID26626129
PMCPMC4767422
OpenAlexW2295594935

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.