7TLM

Structure of Atopobium parvulum SufS

Summary for 7TLM

• Entry DOI: 10.2210/pdb7tlm/pdb
• Descriptor: Cysteine desulfurase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: cysteine desulferase, transferase
• Biological source: Lancefieldella parvula (Atopobium parvulum)
• Total number of polymer chains: 1
• Total formula weight: 49468.05

Authors

Karunakaran, G.,Couture, J.F. (deposition date: 2022-01-18, release date: 2022-02-16, Last modification date: 2023-11-15)

Primary citation

Karunakaran, G.,Yang, Y.,Tremblay, V.,Ning, Z.,Martin, J.,Belaouad, A.,Figeys, D.,Brunzelle, J.S.,Giguere, P.M.,Stintzi, A.,Couture, J.F.
Structural analysis of Atopobium parvulum SufS cysteine desulfurase linked to Crohn's disease.
Febs Lett., 596:898-909, 2022

PubMed Abstract: 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 (H S) microbial producers positively correlate with the severity of the disease. Atopobium parvulum is a key H 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.

PubMed: 35122247
DOI: 10.1002/1873-3468.14295

Experimental method

X-RAY DIFFRACTION (1.8 Å)