8K5I

The structure of SenA in complex with N,N,N-trimethyl-histidine and thioglucose

8K5I の概要

• エントリーDOI: 10.2210/pdb8k5i/pdb
• 分子名称: selenoneine synthase SenA, FE (III) ION, N,N,N-trimethyl-histidine, ... (7 entities in total)
• 機能のキーワード: selenoneine synthase, nonheme iron enzyme, metal binding protein
• 由来する生物種: Variovorax paradoxus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47843.34

構造登録者

Liu, M.,Yang, Y.,Huang, J.-W.,Chen, C.-C.,Guo, R.-T. (登録日: 2023-07-21, 公開日: 2023-12-06, 最終更新日: 2023-12-13)

主引用文献

Liu, M.,Yang, Y.,Huang, J.W.,Dai, L.,Zheng, Y.,Cheng, S.,He, H.,Chen, C.C.,Guo, R.T.
Structural insights into a novel nonheme iron-dependent oxygenase in selenoneine biosynthesis.
Int.J.Biol.Macromol., 256:128428-128428, 2023

PubMed Abstract: Selenoneine (SEN) is a natural histidine derivative with radical-scavenging activity and shows higher antioxidant potential than its sulfur-containing isolog ergothioneine (EGT). Recently, the SEN biosynthetic pathway in Variovorax paradoxus was reported. Resembling EGT biosynthesis, the committed step of SEN synthesis is catalyzed by a nonheme Fe-dependent oxygenase termed SenA. This enzyme catalyzes oxidative carbon‑selenium (C-Se) bond formation to conjugate N-α-trimethyl histidine (TMH) and selenosugar to yield selenoxide; the process parallels the EGT biosynthetic route, in which sulfoxide synthases known as EgtB members catalyze the conjugation of TMH and cysteine or γ-glutamylcysteine to afford sulfoxides. Here, we report the crystal structures of SenA and its complex with TMH and thioglucose (SGlc), an analog of selenoglucose (SeGlc) at high resolution. The overall structure of SenA adopts the archetypical fold of EgtB, which comprises a DinB-like domain and an FGE-like domain. While the TMH-binding site is highly conserved to that of EgtB, a various substrate-enzyme interaction network in the selenosugar-binding site of SenA features a number of water-mediated hydrogen bonds. The obtained structural information is beneficial for understanding the mechanism of SenA-mediated C-Se bond formation.

PubMed: 38013086
DOI: 10.1016/j.ijbiomac.2023.128428

実験手法

X-RAY DIFFRACTION (1.92 Å)