3q9a | pdb_00003q9a

Structure of neuronal nitric oxide synthase in the ferric state in complex with N-5-[2-(ethylsulfanyl)ethanimidoyl]-L-ornithine

spinqualitylabelsall models 3q9a, resolution 2.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3q9a is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, H4B, HEM, JM7, ZN Related: 3jt5, 3q99 Gene: Nos1, Bnos (Rattus norvegicus) Activity: Nitric-oxide synthase, with EC number 1.14.13.39 Resources: FirstGlance, OCA, RCSB, PDBsum Function [NOS1_RAT] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum. Publication Abstract from PubMed A series of l-arginine analogue nitric oxide synthase inhibitors with a thioether tail have been shown to form an Fe-S thioether interaction as evidenced by continuous electron density between the Fe and S atoms. Even so, the Fe-S thioether interaction was found to be far less important for inhibitor binding than the hydrophobic interactions between the alkyl group in the thioether tail and surrounding protein ( Martell et al. J. Am. Chem. Soc. 2010 , 132 , 798 ). However, among the few thioether inhibitors that showed Fe-S thioether interaction in crystal structures, variations in spin state (high-spin or low-spin) were observed dependent upon the heme iron oxidation state and temperature. Since modern synchrotron X-ray data collection is typically carried out at cryogenic temperatures, we reasoned that some of the discrepancies between cryo-crystal structures and room-temperature UV-visible spectroscopy could be the result of temperature-dependent spin-state changes. We, therefore, have characterized some of these neuronal nitric oxide synthase (nNOS)-thioether inhibitor complexes in both crystal and solution using EPR and UV-visible absorption spectrometry as a function of temperature and the heme iron redox state. We found that some thioether inhibitors switch from high to low spin at lower temperatures similar to the "spin crossover" phenomenon observed in many transition metal complexes. Temperature-Dependent Spin Crossover in Neuronal Nitric Oxide Synthase Bound with the Heme-Coordinating Thioether Inhibitors.,Doukov T, Li H, Sharma A, Martell JD, Soltis SM, Silverman RB, Poulos TL J Am Chem Soc. 2011 May 11. PMID:21534614 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nitric Oxide Synthase

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