Evidence map›Paper›PMID 29339766›Full record

ArticleScientific reports2018

The crystal structure of D-xylonate dehydratase reveals functional features of enzymes from the Ilv/ED dehydratase family.

Mohammad Mubinur Rahman, Martina Andberg, Anu Koivula, Juha Rouvinen, Nina Hakulinen

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

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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.

Mohammad Mubinur RahmanDepartment of Chemistry, University of Eastern Finland, PO Box 111, FIN-80101, Joensuu, Finland.
Martina AndbergVTT Technical Research Centre of Finland Ltd, PO Box 1000, FIN-02044 VTT, Espoo, Finland.
Anu KoivulaVTT Technical Research Centre of Finland Ltd, PO Box 1000, FIN-02044 VTT, Espoo, Finland.
Juha RouvinenDepartment of Chemistry, University of Eastern Finland, PO Box 111, FIN-80101, Joensuu, Finland.
Nina HakulinenDepartment of Chemistry, University of Eastern Finland, PO Box 111, FIN-80101, Joensuu, Finland. nina.hakulinen@uef.fi.ORCID http://orcid.org/0000-0003-4471-7188
University of Eastern Finland · FIVTT Technical Research Centre of Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Ilv/ED dehydratase protein family includes dihydroxy acid-, gluconate-, 6-phosphogluconate- and pentonate dehydratases. The members of this family are involved in various biosynthetic and carbohydrate metabolic pathways. Here, we describe the first crystal structure of D-xylonate dehydratase from Caulobacter crescentus (CcXyDHT) at 2.7 Å resolution and compare it with other available enzyme structures from the IlvD/EDD protein family. The quaternary structure of CcXyDHT is a tetramer, and each monomer is composed of two domains in which the N-terminal domain forms a binding site for a [2Fe-2S] cluster and a Mg

Indexed as

Amino Acid MotifsAmino Acid SequenceBinding SitesBiocatalysisCatalytic DomainCaulobacter crescentusCrystallography, X-RayHydro-LyasesMagnesiumProtein Structure, QuaternarySequence AlignmentSubstrate SpecificityD-xylo-aldonate dehydrataseHydro-LyasesMagnesium

Identifiers

PMID29339766
PMCPMC5770437
OpenAlexW2784064341

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.