ATP结合盒运输机
麦角新碱
微生物学
生物
琥珀酰化
结核分枝杆菌
细菌
生物化学
金黄色葡萄球菌
运输机
单核细胞增生李斯特菌
厚壁菌
脂质Ⅱ
化学
细菌细胞结构
乙酰化
抗氧化剂
基因
遗传学
肺结核
病理
医学
16S核糖体RNA
作者
Yifan Zhang,Giovanni González-Gutiérrez,Katherine A. Legg,Brenna J. C. Walsh,C Diez,Katherine A. Edmonds,David P. Giedroc
标识
DOI:10.1038/s41467-022-35277-3
摘要
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.
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