8IRZ

Carbon Sulfoxide lyase

Summary for 8IRZ

• Entry DOI: 10.2210/pdb8irz/pdb
• Descriptor: Probable hercynylcysteine sulfoxide lyase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: lyase, carbon sulfoxide lyase, egte
• Biological source: Mycolicibacterium smegmatis MC2 155
• Total number of polymer chains: 2
• Total formula weight: 83187.57

Authors

Gong, W.M.,Wei, L.L.,Liu, L. (deposition date: 2023-03-20, release date: 2024-03-06, Last modification date: 2024-03-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.86 Å)