3BXV

Crystal structure studies on sulfur oxygenase reductase from Acidianus tengchongensis

Summary for 3BXV

• Entry DOI: 10.2210/pdb3bxv/pdb
• Descriptor: Sulfur oxygenase/reductase, FE (III) ION (3 entities in total)
• Functional Keywords: beta barrel, oxidoreductase
• Biological source: Acidianus tengchongenses
• Total number of polymer chains: 1
• Total formula weight: 35239.30

Authors

Chang, W.R.,Li, M. (deposition date: 2008-01-14, release date: 2009-01-20, Last modification date: 2025-04-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)