5V12

Crystal structure of Carbon Sulfoxide lyase, Egt2 Y134F with sulfenic acid intermediate

5V12 の概要

• エントリーDOI: 10.2210/pdb5v12/pdb
• 分子名称: Hercynylcysteine sulfoxide lyase, FORMIC ACID, (1S)-1-carboxy-2-[2-(hydroxysulfanyl)-1H-imidazol-4-yl]-N,N,N-trimethylethan-1-aminium, ... (5 entities in total)
• 機能のキーワード: c-s lyase, plp dependent, lyase
• 由来する生物種: Neurospora crassa OR74A; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 452357.99

構造登録者

Irani, S.,Zhang, Y. (登録日: 2017-03-01, 公開日: 2018-03-07, 最終更新日: 2024-05-01)

主引用文献

Irani, S.,Naowarojna, N.,Tang, Y.,Kathuria, K.R.,Wang, S.,Dhembi, A.,Lee, N.,Yan, W.,Lyu, H.,Costello, C.E.,Liu, P.,Zhang, Y.J.
Snapshots of C-S Cleavage in Egt2 Reveals Substrate Specificity and Reaction Mechanism.
Cell Chem Biol, 25:519-529.e4, 2018

PubMed Abstract: Sulfur incorporation in the biosynthesis of ergothioneine, a histidine thiol derivative, differs from other well-characterized transsulfurations. A combination of a mononuclear non-heme iron enzyme-catalyzed oxidative C-S bond formation and a subsequent pyridoxal 5'-phosphate (PLP)-mediated C-S lyase reaction leads to the net transfer of a sulfur atom from a cysteine to a histidine. In this study, we structurally and mechanistically characterized a PLP-dependent C-S lyase Egt2, which mediates the sulfoxide C-S bond cleavage in ergothioneine biosynthesis. A cation-π interaction between substrate and enzyme accounts for Egt2's preference of sulfoxide over thioether as a substrate. Using mutagenesis and structural biology, we captured three distinct states of the Egt2 C-S lyase reaction cycle, including a labile sulfenic intermediate captured in Egt2 crystals. Chemical trapping and high-resolution mass spectrometry were used to confirm the involvement of the sulfenic acid intermediate in Egt2 catalysis.

PubMed: 29503207
DOI: 10.1016/j.chembiol.2018.02.002

実験手法

X-RAY DIFFRACTION (2.451 Å)