8IRK

Carbon Sulfoxide lyase

8IRK の概要

• エントリーDOI: 10.2210/pdb8irk/pdb
• 分子名称: Probable hercynylcysteine sulfoxide lyase, PYRIDOXAL-5'-PHOSPHATE, PYRUVIC ACID, ... (4 entities in total)
• 機能のキーワード: lyase
• 由来する生物種: Mycolicibacterium smegmatis MC2 155
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 166591.47

構造登録者

Gong, W.M.,Wei, L.L.,Liu, L. (登録日: 2023-03-18, 公開日: 2024-03-06, 最終更新日: 2024-09-18)

主引用文献

Wei, L.,Liu, L.,Gong, W.
Structure of mycobacterial ergothioneine-biosynthesis C-S lyase EgtE.
J.Biol.Chem., 300:105539-105539, 2024

PubMed Abstract: L-ergothioneine is widely distributed among various microbes to regulate their physiology and pathogenicity within complex environments. One of the key steps in the ergothioneine-biosynthesis pathway, the C-S bond cleavage reaction, uses the pyridoxal 5'-phosphate dependent C-S lyase to produce the final product L-ergothioneine. Here, we present the crystallographic structure of the ergothioneine-biosynthesis C-S lyase EgtE from Mycobacterium smegmatis (MsEgtE) represents the first published structure of ergothioneine-biosynthesis C-S lyases in bacteria and shows the effects of active site residues on the enzymatic reaction. The MsEgtE and the previously reported ergothioneine-biosynthesis C-S lyase Egt2 from Neurospora crassa (NcEgt2) fold similarly. However, discrepancies arise in terms of substrate recognition, as observed through sequence and structure comparison of MsEgtE and NcEgt2. The structural-based sequence alignment of the ergothioneine-biosynthesis C-S lyase from fungi and bacteria shows clear distinctions among the recognized substrate residues, but Arg348 is critical and an extremely conserved residue for substrate recognition. The α14 helix is exclusively found in the bacteria EgtE, which represent the most significant difference between bacteria EgtE and fungi Egt2, possibly resulting from the convergent evolution of bacteria and fungi.

PubMed: 38072054
DOI: 10.1016/j.jbc.2023.105539

実験手法

X-RAY DIFFRACTION (2.35 Å)