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3H8I

The first X-ray structure of a sulfide:quinone oxidoreductase: Insights into sulfide oxidation mechanism

Summary for 3H8I
Entry DOI10.2210/pdb3h8i/pdb
Related3H8L
DescriptorNADH oxidase, FLAVIN-ADENINE DINUCLEOTIDE, trisulfane, ... (5 entities in total)
Functional Keywordsmembrane protein, rossman-like fold, oxidoreductase
Biological sourceAcidianus ambivalens (Desulfurolobus ambivalens)
Total number of polymer chains2
Total formula weight92971.49
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: 2024-11-20)
Primary citationBrito, 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: 19438211
DOI: 10.1021/bi9003827
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.65 Å)
Structure validation

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