7TLQ

Structure of Atopobium parvulum SufS C375S

7TLQ の概要

• エントリーDOI: 10.2210/pdb7tlq/pdb
• 分子名称: Cysteine desulfurase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• 機能のキーワード: cysteine desulferase, transferase
• 由来する生物種: Lancefieldella parvula
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 98839.84

構造登録者

Karunakaran, G.,Couture, J.F. (登録日: 2022-01-18, 公開日: 2022-02-16, 最終更新日: 2023-10-18)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)