Discovery and structure of a widespread bacterial ABC transporter specific for ergothioneine

Yifan Zhang, Giovanni Gonzalez-Gutierrez, Katherine A. Legg, Brenna J. C. Walsh, Cristian M. Pis Diez, Katherine A. Edmonds and David P. Giedroc ()
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Yifan Zhang: Indiana University
Giovanni Gonzalez-Gutierrez: Indiana University
Katherine A. Legg: Indiana University
Brenna J. C. Walsh: Indiana University
Cristian M. Pis Diez: Fundación Instituto Leloir
Katherine A. Edmonds: Indiana University
David P. Giedroc: Indiana University

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract L-Ergothioneine (ET), the 2-thioimidazole derivative of trimethylhistidine, is biosynthesized by select fungi and bacteria, notably Mycobacterium tuberculosis, and functions as a scavenger of reactive oxygen species. The extent to which ET broadly functions in bacterial cells unable to synthesize it is unknown. Here we show that spd_1642-1643 in Streptococcus pneumoniae, a Gram-positive respiratory pathogen, encodes an ET uptake ATP-binding cassette (ABC) transporter, designated EgtU. The solute binding domain (SBD) of EgtU, EgtUC, binds ET with high affinity and exquisite specificity in a cleft between the two subdomains, with cation-π interactions engaging the betaine moiety and a network of water molecules that surround the thioimidazole ring. EgtU is highly conserved among known quaternary amine compound-specific transporters and widely distributed in Firmicutes, including the human pathogens Listeria monocytogenes, as BilEB, Enterococcus faecalis and Staphylococcus aureus. ET increases the chemical diversity of the low molecular weight thiol pool in Gram-positive human pathogens and may contribute to antioxidant defenses in the infected host.

Date: 2022
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DOI: 10.1038/s41467-022-35277-3

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