2YAX
IODOACETAMIDE INHIBITED SULFUR OXYGENASE REDUCTASE
Summary for 2YAX
Entry DOI | 10.2210/pdb2yax/pdb |
Related | 2CB2 2YAV 2YAW |
Descriptor | SULFUR OXYGENASE/REDUCTASE, FE (III) ION, ... (4 entities in total) |
Functional Keywords | oxidoreductase, mononuclear non-heme iron, biogeochemical sulfur cycle, thermophilic, cysteine persulphide, icosatetramer |
Biological source | ACIDIANUS AMBIVALENS More |
Total number of polymer chains | 6 |
Total formula weight | 218984.25 |
Authors | Veith, A.,Urich, T.,Seyfarth, K.,Protze, J.,Frazao, C.,Kletzin, A. (deposition date: 2011-02-25, release date: 2011-12-21, Last modification date: 2023-12-20) |
Primary citation | Veith, A.,Urich, T.,Seyfarth, K.,Protze, J.,Frazao, C.,Kletzin, A. Substrate Pathways and Mechanisms of Inhibition in the Sulfur Oxygenase Reductase of Acidianus Ambivalens. Front.Microbiol., 2:37-, 2011 Cited by PubMed Abstract: The sulfur oxygenase reductase (SOR) is the initial enzyme of the sulfur oxidation pathway in the thermoacidophilic Archaeon Acidianus ambivalens. The SOR catalyzes an oxygen-dependent sulfur disproportionation to H(2)S, sulfite and thiosulfate. The spherical, hollow, cytoplasmic enzyme is composed of 24 identical subunits with an active site pocket each comprising a mononuclear non-heme iron site and a cysteine persulfide. Substrate access and product exit occur via apolar chimney-like protrusions at the fourfold symmetry axes, via narrow polar pores at the threefold symmetry axes and via narrow apolar pores within in each subunit. In order to investigate the function of the pores we performed site-directed mutagenesis and inhibitor studies. PubMed: 21747782DOI: 10.3389/FMICB.2011.00037 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report