1mjt
CRYSTAL STRUCTURE OF SANOS, A BACTERIAL NITRIC OXIDE SYNTHASE OXYGENASE PROTEIN, IN COMPLEX WITH NAD+ AND SEITU
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OverviewOverview
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.
About this StructureAbout this Structure
1MJT is a Single protein structure of sequence from Staphylococcus aureus with SUC, HEM, ITU and NAD as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.
ReferenceReference
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
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