Evidence map›Paper›PMID 17824670›Full record

ArticleBiochemistry2007

Multiple metal binding domains enhance the Zn(II) selectivity of the divalent metal ion transporter AztA.

Tong Liu, Hermes Reyes-Caballero, Chenxi Li, Robert A Scott, David P Giedroc

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Characterization of three predicted zinc exporters inFrontiers in veterinary science · 2023
    Article
  3. Article
  4. Review
  5. Bacterial metallothioneins: past, present, and questions for the future.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011
    Review
  6. NMR structural analysis of the soluble domain of ZiaA-ATPase and the basis of selective interactions with copper metallochaperone Atx1.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. 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

5 authors at 2 institutions in 1 country.

Tong LiuDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128, USA.
Hermes Reyes-Caballero
Chenxi Li
Robert A Scott
David P Giedroc
Texas A&M University · USUniversity of Georgia · US

Funding

ZINC COORDINATION AND REGULATION OF ZINC METALLOPROTEINSR01GM042569 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI GIEDROC, DAVID P. · 1996 to 2015
$4.9M
X-RAY ABSORPTION SPECTROSCOPY OF METALLOENZYMESR01GM042025 · NIGMS · UNIVERSITY OF GEORGIA (UGA) · PI SCOTT, ROBERT A · 1989 to 2010
$2.6M
ZINC DOMAIN STRUCTURE AND FUNCTION IN T4 GENE 32 PROTEINR29GM042569 · NIGMS · TEXAS AGRILIFE RESEARCH · PI GIEDROC, DAVID P. · 1991 to 1995
–
NIGMS NIH HHS GM042025NIGMS NIH HHS GM042569NIGMS NIH HHS R01 GM042025NIGMS NIH HHS R01 GM042569
6 · The paper itself

Abstract

Transition metal-transporting P1B-type CPx ATPases play crucial roles in mediating metal homeostasis and resistance in all cells. The degree to which N-terminal metal binding domains (MBDs) confer metal specificity to the transporter is unclear. We show that the two MBDs of the Zn/Cd/Pb effluxing pump Anabaena AztA are functionally nonequivalent, but only with respect to zinc resistance. Inactivation of the a-MBD largely abrogates resistance to high intracellular Zn(II) levels, whereas inactivation of the b-MBD is not as deleterious. In contrast, inactivation of either the a- or b-MBD has little measurable impact on Cd(II) and Pb(II) resistance. The membrane proximal b-MBD binds Zn(II) with a higher affinity than the distal N-terminal a-MBD. Facile Zn(II)-specific intermolecular transfer from the a-MBD to the higher-affinity b-MBD is readily observed by 1H-15N HSQC spectroscopy. Unlike Zn(II), Cd(II) and Pb(II) form saturated 1:1 S4 or S3(O/N) complexes with AztAaHbH, where a single metal ion bridges the two MBDs. We propose that the tandem MBDs enhance Zn(II)-specific transport, while stabilizing a non-native inter-MBD Cd/Pb cross-linked structure that is a poor substrate and/or regulator for the transporter.

Indexed as

Amino Acid SequenceAnabaenaCadmiumCations, DivalentKineticsLeadMagnetic Resonance SpectroscopyMembrane Transport ProteinsModels, MolecularMolecular Sequence DataProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidZincCadmiumCations, DivalentLeadMembrane Transport ProteinsZinc

Identifiers

PMID17824670
PMCPMC3561713
OpenAlexW1977548575

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.