Evidence map›Paper›PMID 38170898›Full record

ArticleDalton transactions (Cambridge, England : 2003)2024

Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features.

Magali Roger, Philippe Leone, Ninian J Blackburn, Sam Horrell, Tadeo Moreno Chicano, Frédéric Biaso, Marie-Thérèse Giudici-Orticoni, Luciano A Abriata, Greg L Hura, Michael A Hough and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Dalton transactions (Cambridge, England : 2003), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 48% 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

5 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Methionine-rich domains emerge as facilitators of copper recruitment in detoxification systems.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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 4 institutions in 4 countries.

Magali RogerCNRS, Aix-Marseille University, Bioenergetic and Protein Engineering Laboratory, BIP UMR 7281, Mediterranean Institute of Microbiology, 13009 Marseille, France. giuliano.sciara@inrae.fr.
Philippe LeoneCNRS, Aix-Marseille University, Laboratoire d'Ingénierie des Systèmes Macromoléculaires, LISM UMR7255, 13009 Marseille, France.
Ninian J BlackburnDepartment of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, Oregon 97239, USA.
Sam HorrellSchool of Life Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, UK.
Tadeo Moreno ChicanoSchool of Life Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, UK.
Frédéric BiasoCNRS, Aix-Marseille University, Bioenergetic and Protein Engineering Laboratory, BIP UMR 7281, Mediterranean Institute of Microbiology, 13009 Marseille, France. giuliano.sciara@inrae.fr.
Marie-Thérèse Giudici-OrticoniCNRS, Aix-Marseille University, Bioenergetic and Protein Engineering Laboratory, BIP UMR 7281, Mediterranean Institute of Microbiology, 13009 Marseille, France. giuliano.sciara@inrae.fr.
Luciano A AbriataLaboratory for Biomolecular Modeling and Protein Purification and Structure Core Facility, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.ORCID http://orcid.org/0000-0003-3087-8677
Greg L HuraMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Lab, Berkeley, CA, USA.
Michael A HoughSchool of Life Sciences, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, UK.
Giuliano SciaraCNRS, Aix-Marseille University, Bioenergetic and Protein Engineering Laboratory, BIP UMR 7281, Mediterranean Institute of Microbiology, 13009 Marseille, France. giuliano.sciara@inrae.fr.ORCID http://orcid.org/0000-0002-3790-747X
Marianne IlbertCNRS, Aix-Marseille University, Bioenergetic and Protein Engineering Laboratory, BIP UMR 7281, Mediterranean Institute of Microbiology, 13009 Marseille, France. giuliano.sciara@inrae.fr.ORCID http://orcid.org/0000-0002-9070-2334
Centre National de la Recherche Scientifique · FRUniversity of Essex · GBÉcole Polytechnique Fédérale de Lausanne · CHOregon Health & Science University · US

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Ritimukta Sarangi · 2020 to 2026
$43.3M
Peptide Processing by Copper EnzymesR35GM136239 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI Ninian J Blackburn · 2020 to 2026
$3.4M
Towards Accurate Protein Structure Predictions with SAXS Technology (TAPESTRY)R01GM137021 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TSUTAKAWA, SUSAN EMIKO · 2020 to 2023
$1.6M
NIGMS NIH HHS P30 GM133894NIGMS NIH HHS R01 GM137021NIGMS NIH HHS R35 GM136239
6 · The paper itself

Abstract

Cupredoxins are widely occurring copper-binding proteins with a typical Greek-key beta barrel fold. They are generally described as electron carriers that rely on a T1 copper centre coordinated by four ligands provided by the folded polypeptide. The discovery of novel cupredoxins demonstrates the high diversity of this family, with variations in terms of copper-binding ligands, copper centre geometry, redox potential, as well as biological function. AcoP is a periplasmic cupredoxin belonging to the iron respiratory chain of the acidophilic bacterium Acidithiobacillus ferrooxidans. AcoP presents original features, including high resistance to acidic pH and a constrained green-type copper centre of high redox potential. To understand the unique properties of AcoP, we undertook structural and biophysical characterization of wild-type AcoP and of two Cu-ligand mutants (H166A and M171A). The crystallographic structures, including native reduced AcoP at 1.65 Å resolution, unveil a typical cupredoxin fold. The presence of extended loops, never observed in previously characterized cupredoxins, might account for the interaction of AcoP with physiological partners. The Cu-ligand distances, determined by both X-ray diffraction and EXAFS, show that the AcoP metal centre seems to present both T1 and T1.5 features, in turn suggesting that AcoP might not fit well to the coupled distortion model. The crystal structures of two AcoP mutants confirm that the active centre of AcoP is highly constrained. Comparative analysis with other cupredoxins of known structures, suggests that in AcoP the second coordination sphere might be an important determinant of active centre rigidity due to the presence of an extensive hydrogen bond network. Finally, we show that other cupredoxins do not perfectly follow the coupled distortion model as well, raising the suspicion that further alternative models to describe copper centre geometries need to be developed, while the importance of rack-induced contributions should not be underestimated.

Indexed as

AzurinCopperBinding SitesLigandsAzurinCoppercupredoxinLigands

Identifiers

PMID38170898
PMCPMC10804444
OpenAlexW4390532126

What OpenQuestion holds

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LicenceCC BY-NC
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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.