8A56

Coenzyme A-persulfide reductase (CoAPR) from Enterococcus faecalis

8A56 の概要

• エントリーDOI: 10.2210/pdb8a56/pdb
• 分子名称: Coenzyme A-persulfide reductase, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (7 entities in total)
• 機能のキーワード: hydrogen sulfide, coenzyme a, flavoprotein, persulfide reductase
• 由来する生物種: Enterococcus faecalis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 127555.94

構造登録者

Costa, S.S.,Walsh, B.J.,Giedroc, D.P.,Brito, J.A. (登録日: 2022-06-14, 公開日: 2022-09-14, 最終更新日: 2024-01-31)

主引用文献

Walsh, B.J.C.,Costa, S.S.,Edmonds, K.A.,Trinidad, J.C.,Issoglio, F.M.,Brito, J.A.,Giedroc, D.P.
Metabolic and Structural Insights into Hydrogen Sulfide Mis-Regulation in Enterococcus faecalis.
Antioxidants, 11:-, 2022

PubMed Abstract: Hydrogen sulfide (HS) is implicated as a cytoprotective agent that bacteria employ in response to host-induced stressors, such as oxidative stress and antibiotics. The physiological benefits often attributed to HS, however, are likely a result of downstream, more oxidized forms of sulfur, collectively termed reactive sulfur species (RSS) and including the organic persulfide (RSSH). Here, we investigated the metabolic response of the commensal gut microorganism to exogenous NaS as a proxy for HS/RSS toxicity. We found that exogenous sulfide increases protein abundance for enzymes responsible for the biosynthesis of coenzyme A (CoA). Proteome -sulfuration (persulfidation), a posttranslational modification implicated in HS signal transduction, is also widespread in this organism and is significantly elevated by exogenous sulfide in CstR, the RSS sensor, coenzyme A persulfide (CoASSH) reductase (CoAPR) and enzymes associated with de novo fatty acid biosynthesis and acetyl-CoA synthesis. Exogenous sulfide significantly impacts the speciation of fatty acids as well as cellular concentrations of acetyl-CoA, suggesting that protein persulfidation may impact flux through these pathways. Indeed, CoASSH is an inhibitor of phosphotransacetylase (Pta), suggesting that an important metabolic consequence of increased levels of HS/RSS may be over-persulfidation of this key metabolite, which, in turn, inhibits CoA and acyl-CoA-utilizing enzymes. Our 2.05 Å crystallographic structure of CoA-bound CoAPR provides new structural insights into CoASSH clearance in .

PubMed: 36009332
DOI: 10.3390/antiox11081607

実験手法

X-RAY DIFFRACTION (2.05 Å)