3H8L
The first X-ray structure of a sulfide:quinone oxidoreductase: insights into sulfide oxidation mechanism
Summary for 3H8L
| Entry DOI | 10.2210/pdb3h8l/pdb |
| Related | 3H8I |
| Descriptor | NADH oxidase, FLAVIN-ADENINE DINUCLEOTIDE, trisulfane, ... (5 entities in total) |
| Functional Keywords | membrane protein, complete form, rossman-like fold, oxidoreductase |
| Biological source | Acidianus ambivalens (Desulfurolobus ambivalens) |
| Total number of polymer chains | 2 |
| Total formula weight | 92971.49 |
| Authors | Brito, J.A.,Sousa, F.L.,Stelter, M.,Bandeiras, T.M.,Vonrhein, C.,Teixeira, M.,Pereira, M.M.,Archer, M. (deposition date: 2009-04-29, release date: 2009-06-02, Last modification date: 2024-10-16) |
| Primary citation | Brito, J.A.,Sousa, F.L.,Stelter, M.,Bandeiras, T.M.,Vonrhein, C.,Teixeira, M.,Pereira, M.M.,Archer, M. Structural and functional insights into sulfide:quinone oxidoreductase. Biochemistry, 48:5613-5622, 2009 Cited by PubMed Abstract: A sulfide:quinone oxidoreductase (SQR) was isolated from the membranes of the hyperthermoacidophilic archaeon Acidianus ambivalens, and its X-ray structure, the first reported for an SQR, was determined to 2.6 A resolution. This enzyme was functionally and structurally characterized and was shown to have two redox active sites: a covalently bound FAD and an adjacent pair of cysteine residues. Most interestingly, the X-ray structure revealed the presence of a chain of three sulfur atoms bridging those two cysteine residues. The possible implications of this observation in the catalytic mechanism for sulfide oxidation are discussed, and the role of SQR in the sulfur dependent bioenergetics of A. ambivalens, linked to oxygen reduction, is addressed. PubMed: 19438211DOI: 10.1021/bi9003827 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.57 Å) |
Structure validation
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