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

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Karunakaran, Gapisha, Yang, Yidai, Tremblay, Véronique, Ning, Zhibin, Martin, Jade, Belaouad, Amine, Figeys, Daniel, Brunzelle, Joseph S., Giguere, Patrick M., Stintzi, Alain and Couture, Jean François (2022) Structural analysis of Atopobium parvulum SufS cysteine desulfurase linked to Crohn's disease. FEBS Letters, 596 (7). pp. 898-909. ISSN 0014-5793

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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 (H2S) microbial producers positively correlate with the severity of the disease. Atopobium parvulum is a key H2S 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.

Item Type: Article
Additional Information: The atomic coordinates and structure factors of ApSufswild-type and mutants have been deposited to the PDBwith the following accession codes: wild-type–7TLM,C375S mutant–7TLQ, A34Y mutant–7TLR, K235Rmutant–7TLP
Uncontrolled Keywords: atopobium,cysteine desulfurase,inflammatory bowel disease,sufs,x-ray crystallography,biophysics,structural biology,biochemistry,molecular biology,genetics,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1304
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
UEA Research Groups: Faculty of Medicine and Health Sciences > Research Centres > Metabolic Health
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Depositing User: LivePure Connector
Date Deposited: 06 Mar 2026 14:30
Last Modified: 09 Mar 2026 16:31
URI: https://ueaeprints.uea.ac.uk/id/eprint/102240
DOI: 10.1002/1873-3468.14295

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