2icq

urate oxidase under 2.0 MPa pressure of nitrous oxide

spinqualitylabelsall models 2icq, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2icq is a 1 chain structure with sequence from Aspfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AZA, CYS, N2O NonStd Res: ACE Related: 2iba, 2ic0 Activity: Factor independent urate hydroxylase, with EC number 1.7.3.3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. 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 In contrast with most inhalational anesthetics, the anesthetic gases xenon (Xe) and nitrous oxide (N(2)O) act by blocking the N-methyl-d-aspartate (NMDA) receptor. Using x-ray crystallography, we examined the binding characteristics of these two gases on two soluble proteins as structural models: urate oxidase, which is a prototype of a variety of intracellular globular proteins, and annexin V, which has structural and functional characteristics that allow it to be considered as a prototype for the NMDA receptor. The structure of these proteins complexed with Xe and N(2)O were determined. One N(2)O molecule or one Xe atom binds to the same main site in both proteins. A second subsite is observed for N(2)O in each case. The gas-binding sites are always hydrophobic flexible cavities buried within the monomer. Comparison of the effects of Xe and N(2)O on urate oxidase and annexin V reveals an interesting relationship with the in vivo pharmacological effects of these gases, the ratio of the gas-binding sites' volume expansion and the ratio of the narcotic potency being similar. Given these data, we propose that alterations of cytosolic globular protein functions by general anesthetics would be responsible for the early stages of anesthesia such as amnesia and hypnosis and that additional alterations of ion-channel membrane receptor functions are required for deeper effects that progress to "surgical" anesthesia. Protein crystallography under xenon and nitrous oxide pressure: comparison with in vivo pharmacology studies and implications for the mechanism of inhaled anesthetic action.,Colloc'h N, Sopkova-de Oliveira Santos J, Retailleau P, Vivares D, Bonnete F, Langlois d'Estainto B, Gallois B, Brisson A, Risso JJ, Lemaire M, Prange T, Abraini JH Biophys J. 2007 Jan 1;92(1):217-24. Epub 2006 Oct 6. PMID:17028130 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Urate Oxidase

Proteopedia Page Contributors and Editors (what is this?)

OCA