Evidence map›Paper›PMID 35400666›Full record

ArticleActa crystallographica. Section F, Structural biology communications2022

Structure of BrxA from Staphylococcus aureus, a bacilliredoxin involved in redox homeostasis in Firmicutes.

Colin S McHugh, Paul D Cook

Open access · greenAbstract 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 71% 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

2 authors at 1 institution in 1 country.

Colin S McHughDepartment of Chemistry, Grand Valley State University, 1 Campus Drive, Allendale, MI 49401, USA.
Paul D CookDepartment of Chemistry, Grand Valley State University, 1 Campus Drive, Allendale, MI 49401, USA.
Grand Valley State University · US

Funding

Studies of the bacillithiol biosynthesis and utilization enzymesR15GM117488 · NIGMS · GRAND VALLEY STATE UNIVERSITY · PI COOK, PAUL D. · 2016 to 2020
$767k
NIGMS NIH HHS 2R15GM117488NIGMS NIH HHS R15 GM117488
6 · The paper itself

Abstract

Bacilliredoxins are small proteins that are involved in redox homeostasis in bacillithiol-producing bacteria. They reduce mixed bacillithiol disulfides on protected proteins through a disulfide-exchange reaction, restoring the thiol group on the target protein. Bacilliredoxins contain an unusual conserved CGC motif, and their exact catalytic mechanism remains unclear. Here, a 1.6 Å resolution X-ray crystallographic structure of the bacilliredoxin BrxA (YphP) from Staphylococcus aureus is presented. The structure contains bacillithiol in a mixed disulfide with Cys54, as well as a disulfide linkage at Cys56, which may play a role in dimer stabilization. The structure presented here will provide insight into the function of BrxA and other bacilliredoxins.

Indexed as

BacillotaStaphylococcus aureusBacterial ProteinsCrystallography, X-RayDisulfidesHomeostasisOxidation-ReductionBacterial ProteinsDisulfidesbacillithiolBrxAGram-positive bacteriaoxidative stressredox homeostasisStaphylococcus aureusthioredoxins

Identifiers

PMID35400666
PMCPMC8996147
OpenAlexW4220653121

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.