Expression and purification of the intact bacterial ergothioneine transporter EgtU.

Katherine A Edmonds, Karla Diaz-Rodriguez, David P Giedroc

Abstract read

In one paragraph

Article in Protein expression and purification, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

CH•••S hydrogen bonds drive molecular recognition of ergothioneine by the microbial transporter.Science advances · 2026
Article

4 · The record

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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

3 authors.

Katherine A EdmondsDepartment of Chemistry, Indiana University, Bloomington, IN, USA.

Karla Diaz-RodriguezDepartment of Chemistry, Indiana University, Bloomington, IN, USA.

David P GiedrocDepartment of Chemistry, Indiana University, Bloomington, IN, USA. Electronic address: giedroc@iu.edu.

Funding

Transition Metal Homeostasis and Reactive Sulfur Species in Bacterial PathogensR35GM118157 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI DAVID P. GIEDROC · 2016 to 2026

$5.9M

NIGMS NIH HHS R35 GM118157

6 · The paper itself

Abstract

The bacterial ATP-binding cassette (ABC) transporter EgtU is responsible for uptake of the cellular antioxidant ergothioneine in Streptococcus pneumoniae, and it has homologs in a surprisingly diverse range of microbial pathogens. Crystal structures have been reported for the solute binding domain of EgtU, but many details of the structure and function of the intact heterotetrameric transporter remain to be elucidated. In this study, we have expressed S. pneumoniae EgtU and purified it from E. coli BL21 (DE3) with high purity and homogeneity. Our preliminary data establish ergothioneine binding and ATP hydrolysis by the full-length transporter solubilized in DDM micelles. Our workflow allows for isolation of suitable quantities of EgtU for ongoing structural studies and detailed biophysical characterization.

Indexed as

ATP-Binding Cassette TransportersBacterial ProteinsErgothioneineEscherichia coliStreptococcus pneumoniaeAdenosine TriphosphateCloning, MolecularGene ExpressionRecombinant ProteinsAdenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsErgothioneineRecombinant ProteinsABC transporterEgtUErgothioneine

Identifiers

PMID39577818

DOI10.1016/j.pep.2024.106633

PMCPMC11685028

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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.