Structural highlights
Function
[NOSO_STAAU] Catalyzes the production of nitric oxide (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Prokaryotic genes related to the oxygenase domain of mammalian nitric oxide synthases (NOSs) have recently been identified. Although they catalyze the same reaction as the eukaryotic NOS oxygenase domain, their biological function(s) are unknown. In order to explore rationally the biochemistry and evolution of the prokaryotic NOS family, we have determined the crystal structure of SANOS, from methicillin-resistant Staphylococcus aureus (MRSA), to 2.4 A. Haem and S-ethylisothiourea (SEITU) are bound at the SANOS active site, while the intersubunit site, occupied by the redox cofactor tetrahydrobiopterin (H(4)B) in mammalian NOSs, has NAD(+) bound in SANOS. In common with all bacterial NOSs, SANOS lacks the N-terminal extension responsible for stable dimerization in mammalian isoforms, but has alternative interactions to promote dimer formation.
Crystal structure of SANOS, a bacterial nitric oxide synthase oxygenase protein from Staphylococcus aureus.,Bird LE, Ren J, Zhang J, Foxwell N, Hawkins AR, Charles IG, Stammers DK Structure. 2002 Dec;10(12):1687-96. PMID:12467576[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bird LE, Ren J, Zhang J, Foxwell N, Hawkins AR, Charles IG, Stammers DK. Crystal structure of SANOS, a bacterial nitric oxide synthase oxygenase protein from Staphylococcus aureus. Structure. 2002 Dec;10(12):1687-96. PMID:12467576
