3BXV

Crystal structure studies on sulfur oxygenase reductase from Acidianus tengchongensis

3BXV の概要

• エントリーDOI: 10.2210/pdb3bxv/pdb
• 分子名称: Sulfur oxygenase/reductase, FE (III) ION (3 entities in total)
• 機能のキーワード: beta barrel, oxidoreductase
• 由来する生物種: Acidianus tengchongenses
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35239.30

構造登録者

Chang, W.R.,Li, M. (登録日: 2008-01-14, 公開日: 2009-01-20, 最終更新日: 2025-04-30)

主引用文献

Li, M.,Chen, Z.,Zhang, P.,Pan, X.,Jiang, C.,An, X.,Liu, S.,Chang, W.
Crystal structure studies on sulfur oxygenase reductase from Acidianus tengchongensis
Biochem.Biophys.Res.Commun., 369:919-923, 2008

PubMed Abstract: Sulfur oxygenase reductase (SOR) simultaneously catalyzes oxidation and reduction of elemental sulfur to produce sulfite, thiosulfate, and sulfide in the presence of molecular oxygen. In this study, crystal structures of wild type and mutants of SOR from Acidianus tengchongensis (SOR-AT) in two different crystal forms were determined and it was observed that 24 identical SOR monomers form a hollow sphere. Within the icosatetramer sphere, the tetramer and trimer channels were proposed as the paths for the substrate and products, respectively. Moreover, a comparison of SOR-AT with SOR-AA (SOR from Acidianus ambivalens) structures showed that significant differences existed at the active site. Firstly, Cys31 is not persulfurated in SOR-AT structures. Secondly, the iron atom is five-coordinated rather than six-coordinated, since one of the water molecules ligated to the iron atom in the SOR-AA structure is lost. Consequently, the binding sites of substrates and a hypothetical catalytic process of SOR were proposed.

PubMed: 18329378
DOI: 10.1016/j.bbrc.2008.02.131

実験手法

X-RAY DIFFRACTION (2.7 Å)