Evidence map›Paper›PMID 32356525›Full record

ArticleActa crystallographica. Section F, Structural biology communications2020

Crystal structure of gluconate 5-dehydrogenase from Lentibacter algarum.

Dengke Tian, Xueqi Fu, Wenqiang Cao, Hong Yuan

Open access · greenAbstract 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
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0citing papers in PubMed
–field-weighted citation impact, top 97% 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

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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

4 authors at 2 institutions in 1 country.

Dengke TianSchool of Life Sciences, Jilin University, Changchun, Jilin 130012, People's Republic of China.
Xueqi FuSchool of Life Sciences, Jilin University, Changchun, Jilin 130012, People's Republic of China.
Wenqiang CaoSchool of Life Sciences, Jilin University, Changchun, Jilin 130012, People's Republic of China.
Hong YuanSchool of Food Science and Engineering, South China University of Technology, Guangzhou, Guangdong 510641, People's Republic of China.
Jilin University · CNSouth China University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gluconate 5-dehydrogenase (Ga5DH; EC 1.1.1.69) from Lentibacter algarum (LaGa5DH) was recombinantly expressed in Escherichia coli and purified to homogeneity. The protein was crystallized and the crystal structure was solved at 2.1 Å resolution. The crystal belonged to the monoclinic system, with space group P1 and unit-cell parameters a = 55.42, b = 55.48, c = 79.16 Å, α = 100.51, β = 105.66, γ = 97.99°. The structure revealed LaGaDH to be a tetramer, with each subunit consisting of six α-helices and three antiparallel β-hairpins. LaGa5DH has high structural similarity to other Ga5DH proteins, demonstrating that this enzyme is highly conserved.

Indexed as

Amino Acid SequenceBacterial ProteinsCrystallizationCrystallography, X-RayEscherichia coliModels, MolecularOxidoreductasesPhylogenyProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein MultimerizationRecombinant ProteinsRhodobacteraceaeSequence AlignmentBacterial Proteinsgluconate 5-dehydrogenaseOxidoreductasesRecombinant Proteinscrystal structuregluconate 5-dehydrogenaseLentibacter algarum

Identifiers

PMID32356525
PMCPMC7193515
OpenAlexW3021431063

What OpenQuestion holds

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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.