Evidence map›Paper›PMID 41834538›Full record

ArticleActa crystallographica. Section D, Structural biology2026

Molecular structure and nickel-binding capacity of Proteus mirabilis UreE.

Jiayi Pan, Sarah L Mueller, Nuren Tasneem, Yang Wu, Emily J Furlong

Abstract read
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In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2026. 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
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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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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.

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.

Jiayi PanDivision of Biomedical Science and Biochemistry, Research School of Biology, Australian National University, Canberra, ACT, Australia.
Sarah L MuellerDivision of Biomedical Science and Biochemistry, Research School of Biology, Australian National University, Canberra, ACT, Australia.
Nuren TasneemDivision of Plant Sciences, Research School of Biology, Australian National University, Canberra, ACT, Australia.
Yang WuResearch School of Earth Sciences, Australian National University, Canberra, ACT, Australia.
Emily J FurlongDivision of Biomedical Science and Biochemistry, Research School of Biology, Australian National University, Canberra, ACT, Australia.

Funding

Australian Institute of Nuclear Science and Engineering ALNSTU25121
6 · The paper itself

Abstract

UreE is a nickel chaperone that is required for the safe and efficient delivery of nickel to the active site of the metalloenzyme urease, which is a key virulence factor of the urinary-tract pathogen Proteus mirabilis. We investigated the structural features of P. mirabilis UreE (PmUreE) using protein X-ray crystallography and its nickel-binding capacity by inductively coupled plasma mass spectrometry. Here, we report a 2.0 Å resolution crystal structure of homodimeric PmUreE and show that it has the capacity to bind five Ni(II) ions per dimer. Truncation of the histidine-rich C-terminus reduced the nickel-binding capacity by two Ni(II) ions per dimer, and comparison with homologous UreE structures allowed the assignment of putative nickel-binding sites within the PmUreE structure. These findings increase our understanding of how PmUreE binds nickel and ultimately prevents this toxic metal from causing significant cellular damage in P. mirabilis.

Indexed as

Bacterial ProteinsMolecular ChaperonesNickelProteus mirabilisBinding SitesCarrier ProteinsCrystallography, X-RayModels, MolecularProtein BindingProtein ConformationBacterial ProteinsCarrier ProteinsMolecular ChaperonesNickelUreE protein, Bacteriametalloproteinsnickel chaperonesProteus mirabilis

Identifiers

PMID41834538
PMCPMC13044922

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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.