2YAV

ZN INHIBITED SULFUR OXYGENASE REDUCTASE

Summary for 2YAV

• Entry DOI: 10.2210/pdb2yav/pdb
• Related: 2CB2 2Y9W 2Y9X 2YAW 2YAX
• Descriptor: SULFUR OXYGENASE/REDUCTASE, FE (III) ION, ZINC ION, ... (6 entities in total)
• Functional Keywords: oxidoreductase, mononuclear non- heme iron, biogeochemical sulfur cycle, thermophilic, cysteine persulphide, icosatetramer
• Biological source: ACIDIANUS AMBIVALENS
• Total number of polymer chains: 6
• Total formula weight: 219772.53

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: 2024-11-20)

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

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: 21747782
DOI: 10.3389/FMICB.2011.00037

Experimental method

X-RAY DIFFRACTION (1.701 Å)