8VIG

EgtB-IV from Geminocystis sp. isolate SKYG4, an ergothioneine-biosynthetic type IV sulfoxide synthase in complex with hercynine

8VIG の概要

• エントリーDOI: 10.2210/pdb8vig/pdb
• 分子名称: Sulfoxide synthase EgtB-IV, FE (III) ION, N,N,N-trimethyl-histidine, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, ergothioneine, sulfoxide, sulfur, non-heme iron
• 由来する生物種: Geminocystis sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55721.89

構造登録者

Ireland, K.A.,Davis, K.M. (登録日: 2024-01-04, 公開日: 2024-08-07, 最終更新日: 2024-11-20)

主引用文献

Ireland, K.A.,Kayrouz, C.M.,Abbott, M.L.,Seyedsayamdost, M.R.,Davis, K.M.
Structural insights into the convergent evolution of sulfoxide synthase EgtB-IV, an ergothioneine-biosynthetic homolog of ovothiol synthase OvoA.
Structure, 32:2013-2022.e5, 2024

PubMed Abstract: Non-heme iron-dependent sulfoxide/selenoxide synthases (NHISS) constitute a unique metalloenzyme class capable of installing a C-S/Se bond onto histidine to generate thio/selenoimidazole antioxidants, such as ergothioneine and ovothiol. These natural products are increasingly recognized for their health benefits. Among associated ergothioneine-biosynthetic enzymes, type IV EgtBs stand out, as they exhibit low sequence similarity with other EgtB subfamilies due to their recent divergence from the ovothiol-biosynthetic enzyme OvoA. Herein, we present crystal structures of two representative EgtB-IV enzymes, offering insights into the basis for this evolutionary convergence and enhancing our understanding of NHISS active site organization more broadly. The ability to interpret how key residues modulate substrate specificity and regioselectivity has implications for downstream identification of divergent reactivity within the NHISS family. To this end, we identify a previously unclassified clade of OvoA-like enzymes with a seemingly hybrid set of characteristics, suggesting they may represent an evolutionary intermediate between OvoA and EgtB-IV.

PubMed: 39216472
DOI: 10.1016/j.str.2024.08.006

実験手法

X-RAY DIFFRACTION (1.6 Å)