4FX9

Structure of the Pyrococcus horikoshii CoA persulfide/polysulfide reductase

4FX9 の概要

• エントリーDOI: 10.2210/pdb4fx9/pdb
• 分子名称: Coenzyme A disulfide reductase, FLAVIN-ADENINE DINUCLEOTIDE, COENZYME A, ... (4 entities in total)
• 機能のキーワード: reductase, disulfide, persulfide, polysulfide, oxidoreductase
• 由来する生物種: Pyrococcus horikoshii OT3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103323.48

構造登録者

Herwald, S.,Lopez, K.M.,Crane III, E.J.,Sazinsky, M.H. (登録日: 2012-07-02, 公開日: 2013-04-10, 最終更新日: 2023-09-13)

主引用文献

Herwald, S.,Liu, A.Y.,Zhu, B.E.,Sea, K.W.,Lopez, K.M.,Sazinsky, M.H.,Crane, E.J.
Structure and substrate specificity of the pyrococcal coenzyme A disulfide reductases/polysulfide reductases (CoADR/Psr): implications for S(0)-based respiration and a sulfur-dependent antioxidant system in Pyrococcus.
Biochemistry, 52:2764-2773, 2013

PubMed Abstract: FAD and NAD(P)H-dependent coenzyme A disulfide reductases/polysulfide reductases (CoADR/Psr) have been proposed to be important for the reduction of sulfur and disulfides in the sulfur-reducing anaerobic hyperthermophiles Pyrococcus horikoshii and Pyrococcus furiosus; however, the form(s) of sulfur that the enzyme actually reduces are not clear. Here we determined the structure for the FAD- and coenzyme A-containing holoenzyme from P. horikoshii to 2.7 Å resolution and characterized its substrate specificity. The enzyme is relatively promiscuous and reduces a range of disulfide, persulfide, and polysulfide compounds. These results indicate that the likely in vivo substrates are NAD(P)H and di-, poly-, and persulfide derivatives of coenzyme A, although polysulfide itself is also efficiently reduced. The role of the enzyme in the reduction of elemental sulfur (S(8)) in situ is not, however, ruled out by these results, and the possible roles of this substrate are discussed. During aerobic persulfide reduction, rapid recycling of the persulfide substrate was observed, which is proposed to occur via sulfide oxidation by O(2) and/or H(2)O(2). As expected, this reaction disappears under anaerobic conditions and may explain observations by others that CoADR is not essential for S(0) respiration in Pyrococcus or Thermococcus but appears to participate in oxidative defense in the presence of S(0). When compared to the homologous Npsr enzyme from Shewanella loihica PV-4 and homologous enzymes known to reduce CoA disulfide, the phCoADR structure shows a relatively restricted substrate channel leading into the sulfur-reducing side of the FAD isoalloxazine ring, suggesting how this enzyme class may select for specific disulfide substrates.

PubMed: 23530771
DOI: 10.1021/bi3014399

実験手法

X-RAY DIFFRACTION (2.7 Å)