Structural analysis of Atopobium parvulum SufS cysteine desulfurase linked to Crohn's disease.

Gapisha Karunakaran, Yidai Yang, Véronique Tremblay, Zhibin Ning, Jade Martin, Amine Belaouad, Daniel Figeys, Joseph S Brunzelle, Patrick M Giguere, Alain Stintzi, Jean-François Couture

FEBS letters 2022 Apr

filter terms:

Crohn's disease (CD) is characterized by the chronic inflammation of the gastrointestinal tract. A dysbiotic microbiome and a defective immune system are linked to CD, where hydrogen sulfide (H2 S) microbial producers positively correlate with the severity of the disease. Atopobium parvulum is a key H2 S producer from the microbiome of CD patients. In this study, the biochemical characterization of two Atopobium parvulum cysteine desulfurases, ApSufS and ApCsdB, shows that the enzymes are allosterically regulated. Structural analyses reveal that ApSufS forms a dimer with conserved characteristics observed in type II cysteine desulfurases. Four residues surrounding the active site are essential to catalyse cysteine desulfurylation, and a segment of short-chain residues grant access for substrate binding. A better understanding of ApSufS will help future avenues for CD treatment. © 2022 Federation of European Biochemical Societies.

Citation

Gapisha Karunakaran, Yidai Yang, Véronique Tremblay, Zhibin Ning, Jade Martin, Amine Belaouad, Daniel Figeys, Joseph S Brunzelle, Patrick M Giguere, Alain Stintzi, Jean-François Couture. Structural analysis of Atopobium parvulum SufS cysteine desulfurase linked to Crohn's disease. FEBS letters. 2022 Apr;596(7):898-909