Evidence map›Paper›PMID 36214476›Full record

ArticleAngewandte Chemie (International ed. in English)2022

Substrate Induced Movement of the Metal Cofactor between Active and Resting State.

Stefan R Marsden, Hein J Wijma, Michael K F Mohr, Inês Justo, Peter-Leon Hagedoorn, Jesper Laustsen, Cy M Jeffries, Dmitri Svergun, Luuk Mestrom, Duncan G G McMillan and 2 more

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

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 58% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. The metal cofactor: stationary or mobile?Applied microbiology and biotechnology · 2024
    Review
  2. Substrate Induced Movement of the Metal Cofactor between Active and Resting State.Angewandte Chemie (International ed. in English) · 2022
    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

12 authors at 3 institutions in 2 countries.

Stefan R MarsdenBiokatalyse, Afdeling Biotechnologie, Technische Universiteit Delft, van der Maasweg 9, 2629HZ, Delft, The Netherlands.
Hein J WijmaGroningen Biomolecular Sciences and Biotechnology Institute, Faculty of Science and Engineering, University of Groningen, Nijenborg 4, 9747AG, Groningen, The Netherlands.ORCID 0000-0003-0891-6972
Michael K F MohrBiokatalyse, Afdeling Biotechnologie, Technische Universiteit Delft, van der Maasweg 9, 2629HZ, Delft, The Netherlands.
Inês JustoEMBL Hamburg, Notkestrasse 85, 22607, Hamburg, Germany.
Peter-Leon HagedoornBiokatalyse, Afdeling Biotechnologie, Technische Universiteit Delft, van der Maasweg 9, 2629HZ, Delft, The Netherlands.ORCID 0000-0001-6342-2022
Jesper LaustsenEMBL Hamburg, Notkestrasse 85, 22607, Hamburg, Germany.
Cy M JeffriesEMBL Hamburg, Notkestrasse 85, 22607, Hamburg, Germany.
Dmitri SvergunEMBL Hamburg, Notkestrasse 85, 22607, Hamburg, Germany.ORCID 0000-0003-0830-5696
Luuk MestromBiokatalyse, Afdeling Biotechnologie, Technische Universiteit Delft, van der Maasweg 9, 2629HZ, Delft, The Netherlands.
Duncan G G McMillanBiokatalyse, Afdeling Biotechnologie, Technische Universiteit Delft, van der Maasweg 9, 2629HZ, Delft, The Netherlands.ORCID 0000-0001-6614-4494
Isabel BentoEMBL Hamburg, Notkestrasse 85, 22607, Hamburg, Germany.ORCID 0000-0003-3801-4929
Ulf HanefeldBiokatalyse, Afdeling Biotechnologie, Technische Universiteit Delft, van der Maasweg 9, 2629HZ, Delft, The Netherlands.ORCID 0000-0002-4102-6165
Delft University of Technology · NLEuropean Molecular Biology Laboratory · DEUniversity of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulation of enzyme activity is vital for living organisms. In metalloenzymes, far-reaching rearrangements of the protein scaffold are generally required to tune the metal cofactor's properties by allosteric regulation. Here structural analysis of hydroxyketoacid aldolase from Sphingomonas wittichii RW1 (SwHKA) revealed a dynamic movement of the metal cofactor between two coordination spheres without protein scaffold rearrangements. In its resting state configuration (M

Indexed as

MetalloproteinsAllosteric RegulationFructose-Bisphosphate AldolaseMetalsFructose-Bisphosphate AldolaseMetalloproteinsMetalsAldol ReactionClass II AldolaseMn MetalloenzymeReaction MechanismStructure

Identifiers

PMID36214476
PMCPMC10099721
OpenAlexW4304112149

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.