Evidence map›Paper›PMID 35234138›Full record

ArticleActa crystallographica. Section F, Structural biology communications2022

Conformational flexibility in the zinc solute-binding protein ZnuA.

Elsie Laban Yekwa, Fred Allen Serrano, Erik Yukl

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

Article in Acta crystallographica. Section F, Structural biology communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 62% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

3 authors at 1 institution in 1 country.

Elsie Laban YekwaDepartment of Chemistry and Biochemistry, New Mexico State University, 1175 North Horseshoe Drive, Las Cruces, NM 88003, USA.ORCID 0000-0001-9038-0366
Fred Allen SerranoDepartment of Chemistry and Biochemistry, New Mexico State University, 1175 North Horseshoe Drive, Las Cruces, NM 88003, USA.
Erik YuklDepartment of Chemistry and Biochemistry, New Mexico State University, 1175 North Horseshoe Drive, Las Cruces, NM 88003, USA.ORCID 0000-0001-6519-6938
New Mexico State University · US

Funding

Periplasmic Zinc Management and Homeostasis in Paracoccus denitrificansR01GM122819 · NIGMS · NEW MEXICO STATE UNIVERSITY LAS CRUCES · PI YUKL, ERIK T · 2018 to 2022
$1.4M
Pilatus 6mS10OD021832 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI ADAMS, PAUL DAVID · 2016 to 2016
$980k
National Institutes of Health, National Institute of General Medical Sciences 1R01GM122819NIGMS NIH HHS R01 GM122819NIH HHS S10 OD021832
6 · The paper itself

Abstract

Zinc is an essential metal for all kingdoms of life, making its transport across the cell membrane a critical function. In bacteria, high-affinity zinc import is accomplished by ATP-binding cassette (ABC) transporters, which rely on extracellular solute-binding proteins (SBPs) of cluster A-I to acquire the metal and deliver it to the membrane permease. These systems are important for survival and virulence, making them attractive targets for the development of novel antibiotics. Citrobacter koseri is an emerging pathogen with extensive antibiotic resistance. High-affinity zinc binding to the C. koseri cluster A-I SBP ZnuA has been characterized and the structure of the zinc-bound (holo) form has been determined by X-ray crystallography. Remarkably, despite 95% sequence identity to the ZnuA homologue from Salmonella enterica, C. koseri ZnuA exhibits a different zinc-coordination environment and a closed rather than an open conformation. Comparison with structures of another close ZnuA homologue from Escherichia coli suggests a surprisingly flexible conformational landscape that may be important for efficient zinc binding and/or delivery to the membrane permease.

Indexed as

ATP-Binding Cassette TransportersZincBacterial ProteinsCrystallography, X-RayEscherichia coliModels, MolecularATP-Binding Cassette TransportersBacterial ProteinsZincATP-binding cassette transportersCitrobacter koserisolute-binding proteinszincZnuA

Identifiers

PMID35234138
PMCPMC8900738
OpenAlexW4214540785

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.