6H99

Crystal structure of anaerobic ergothioneine biosynthesis enzyme from Chlorobium limicola in persulfide form.

Summary for 6H99

• Entry DOI: 10.2210/pdb6h99/pdb
• Descriptor: Sulfurtransferase, MAGNESIUM ION, CHLORIDE ION, ... (7 entities in total)
• Functional Keywords: metabolic role: anaerobic ergothioneine biosynthesis chemical activity: sulfur transfer, c-s bond formation protein family: rhodanese-like enzyme (pf00581), transferase
• Biological source: Chlorobium limicola
• Total number of polymer chains: 1
• Total formula weight: 50557.93

Authors

Leisinger, F.,Burn, R.,Meury, M.,Lukat, P.,Seebeck, F.P. (deposition date: 2018-08-03, release date: 2019-06-12, Last modification date: 2024-11-20)

Primary citation

Leisinger, F.,Burn, R.,Meury, M.,Lukat, P.,Seebeck, F.P.
Structural and Mechanistic Basis for Anaerobic Ergothioneine Biosynthesis.
J.Am.Chem.Soc., 141:6906-6914, 2019

PubMed Abstract: Ergothioneine is an emergent factor in cellular redox biochemistry in humans and pathogenic bacteria. Broad consensus has formed around the idea that ergothioneine protects cells against reactive oxygen species. The recent discovery that anaerobic microorganisms make the same metabolite using oxygen-independent chemistry indicates that ergothioneine also plays physiological roles under anoxic conditions. In this report, we describe the crystal structure of the anaerobic ergothioneine biosynthetic enzyme EanB from green sulfur bacterium Chlorobium limicola. This enzyme catalyzes the oxidative sulfurization of N-α-trimethyl histidine. On the basis of structural and kinetic evidence, we describe the catalytic mechanism of this unusual C-S bond-forming reaction. Significant active-site conservation among distant EanB homologues suggests that the oxidative sulfurization of heterocyclic substrates may occur in a broad range of bacteria.

PubMed: 30943021
DOI: 10.1021/jacs.8b12596

Experimental method

X-RAY DIFFRACTION (1.6 Å)