Evidence map›Paper›PMID 23042995›Full record

ArticleJournal of bacteriology2012

Biophysical and bioinformatic analyses implicate the Treponema pallidum Tp34 lipoprotein (Tp0971) in transition metal homeostasis.

Chad A Brautigam, Ranjit K Deka, Zhiming Ouyang, Mischa Machius, Gregory Knutsen, Diana R Tomchick, Michael V Norgard

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

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  15. Purification, crystallization and preliminary X-ray analysis of TP0435 (Tp17) from the syphilis spirochete Treponema pallidum.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
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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

7 authors at 1 institution in 1 country.

Chad A BrautigamDepartment of Biophysics, The University of Texas Southwestern Medical Center, Dallas, Texas, USA.
Ranjit K Deka
Zhiming Ouyang
Mischa Machius
Gregory Knutsen
Diana R Tomchick
Michael V Norgard
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 R01 AI056305NIAID NIH HHS R01-AI056305
6 · The paper itself

Abstract

Metal ion homeostasis is a critical function of many integral and peripheral membrane proteins. The genome of the etiologic agent of syphilis, Treponema pallidum, is compact and devoid of many metabolic enzyme genes. Nevertheless, it harbors genes coding for homologs of several enzymes that typically require either iron or zinc. The product of the tp0971 gene of T. pallidum, designated Tp34, is a periplasmic lipoprotein that is thought to be tethered to the inner membrane of this organism. Previous work on a water-soluble (nonacylated) recombinant version of Tp34 established that this protein binds to Zn(2+), which, like other transition metal ions, stabilizes the dimeric form of the protein. In this study, we employed analytical ultracentrifugation to establish that four transition metal ions (Ni(2+), Co(2+), Cu(2+), and Zn(2+)) readily induce the dimerization of Tp34; Cu(2+) (50% effective concentration [EC(50)] = 1.7 μM) and Zn(2+) (EC(50) = 6.2 μM) were the most efficacious of these ions. Mutations of the crystallographically identified metal-binding residues hindered the ability of Tp34 to dimerize. X-ray crystallography performed on crystals of Tp34 that had been incubated with metal ions indicated that the binding site could accommodate the metals examined. The findings presented herein, coupled with bioinformatic analyses of related proteins, point to Tp34's likely role in metal ion homeostasis in T. pallidum.

Indexed as

Binding SitesBiological TransportCobaltComputational BiologyCopperCrystallography, X-RayDimerizationGenes, BacterialLipoproteinsMembrane ProteinsMetalsMultigene FamilyMutationNickelProtein BindingProtein MultimerizationCobaltCopperLipoproteinsMembrane ProteinsMetalsNickelZinc

Identifiers

PMID23042995
PMCPMC3510569
OpenAlexW2150500436

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.