Asset Details
Do you wish to reserve the book?
Discovery and structure of a widespread bacterial ABC transporter specific for ergothioneine
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Discovery and structure of a widespread bacterial ABC transporter specific for ergothioneine
Do you wish to request the book?
Discovery and structure of a widespread bacterial ABC transporter specific for ergothioneine
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Discovery and structure of a widespread bacterial ABC transporter specific for ergothioneine
2022
Overview
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.
The extent to which human bacterial pathogens broadly utilize ergothioneine as an antioxidant is unknown. Here, authors describe the discovery of a specific transporter for ergothioneine in a respiratory pathogen that is highly conserved among Firmicutes.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
