8DP7
Structure of Helicobacter pylori EgtU bound to EGT
8DP7 の概要
| エントリーDOI | 10.2210/pdb8dp7/pdb |
| 分子名称 | Osmoprotection protein, trimethyl-[(2S)-1-oxidanyl-1-oxidanylidene-3-(2-sulfanylidene-1,3-dihydroimidazol-4-yl)propan-2-yl]azanium (2 entities in total) |
| 機能のキーワード | egtu, egt, transporter, abc transporter, transport protein |
| 由来する生物種 | Helicobacter pylori (strain P12) |
| タンパク質・核酸の鎖数 | 5 |
| 化学式量合計 | 158957.71 |
| 構造登録者 | |
| 主引用文献 | Dumitrescu, D.G.,Gordon, E.M.,Kovalyova, Y.,Seminara, A.B.,Duncan-Lowey, B.,Forster, E.R.,Zhou, W.,Booth, C.J.,Shen, A.,Kranzusch, P.J.,Hatzios, S.K. A microbial transporter of the dietary antioxidant ergothioneine. Cell, 185:4526-4540.e18, 2022 Cited by PubMed Abstract: Low-molecular-weight (LMW) thiols are small-molecule antioxidants required for the maintenance of intracellular redox homeostasis. However, many host-associated microbes, including the gastric pathogen Helicobacter pylori, unexpectedly lack LMW-thiol biosynthetic pathways. Using reactivity-guided metabolomics, we identified the unusual LMW thiol ergothioneine (EGT) in H. pylori. Dietary EGT accumulates to millimolar levels in human tissues and has been broadly implicated in mitigating disease risk. Although certain microorganisms synthesize EGT, we discovered that H. pylori acquires this LMW thiol from the host environment using a highly selective ATP-binding cassette transporter-EgtUV. EgtUV confers a competitive colonization advantage in vivo and is widely conserved in gastrointestinal microbes. Furthermore, we found that human fecal bacteria metabolize EGT, which may contribute to production of the disease-associated metabolite trimethylamine N-oxide. Collectively, our findings illustrate a previously unappreciated mechanism of microbial redox regulation in the gut and suggest that inter-kingdom competition for dietary EGT may broadly impact human health. PubMed: 36347253DOI: 10.1016/j.cell.2022.10.008 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.35 Å) |
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