Evidence map›Paper›PMID 33006577›Full record

ArticleActa crystallographica. Section F, Structural biology communications2020

Crystal structure of XCC3289 from Xanthomonas campestris: homology with the N-terminal substrate-binding domain of Lon peptidase.

Rahul Singh, Sonali Deshmukh, Ashwani Kumar, Venuka Durani Goyal, Ravindra D Makde

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

Article in Acta crystallographica. Section F, Structural biology communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 91% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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.

Rahul SinghBeamline Development and Application Section, Bhabha Atomic Research Centre, Mumbai 400 085, India.
Sonali DeshmukhBeamline Development and Application Section, Bhabha Atomic Research Centre, Mumbai 400 085, India.
Ashwani KumarBeamline Development and Application Section, Bhabha Atomic Research Centre, Mumbai 400 085, India.
Venuka Durani GoyalBeamline Development and Application Section, Bhabha Atomic Research Centre, Mumbai 400 085, India.
Ravindra D MakdeBeamline Development and Application Section, Bhabha Atomic Research Centre, Mumbai 400 085, India.
Bhabha Atomic Research Centre · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LonA peptidase is a major component of the protein quality-control mechanism in both prokaryotes and the organelles of eukaryotes. Proteins homologous to the N-terminal domain of LonA peptidase, but lacking its other domains, are conserved in several phyla of prokaryotes, including the Xanthomonadales order. However, the function of these homologous proteins (LonNTD-like proteins) is not known. Here, the crystal structure of the LonNTD-like protein from Xanthomonas campestris (XCC3289; UniProt Q8P5P7) is reported at 2.8 Å resolution. The structure was solved by molecular replacement and contains one polypeptide in the asymmetric unit. The structure was refined to an R

Indexed as

Bacterial ProteinsCatalytic DomainCrystallography, X-RayProtease LaProtein BindingProtein ConformationProtein DomainsSubstrate SpecificityXanthomonas campestrisBacterial ProteinsProtease LacereblonLonAprotein bindingXanthomonas campestrisXCC3289

Identifiers

PMID33006577
PMCPMC7531242
OpenAlexW3087987260

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.