4n1g

Crystal Structure of Ca(2+)- discharged F88Y obelin mutant from Obelia longissima at 1.50 Angstrom resolution

spinqualitylabelsall models 4n1g, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4n1g is a 2 chain structure with sequence from Obelia longissima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CEI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function OBL_OBELO Ca(2+)-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of calcium ion trigger the intramolecular oxidation of the chromophore, coelenterazine into coelenteramide and CO(2) with the concomitant emission of light. Publication Abstract from PubMed Ca2+ -regulated photoproteins are responsible for the bioluminescence of a variety of marine coelenterates. All hydromedusan photoproteins are a single-chain polypeptide to which 2-hydroperoxycoelenterazine is tightly but non-covalently bound. Bioluminescence results from oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. The bioluminescence spectral maxima of recombinant photoproteins vary in the range 462-495 nm, despite a high degree of identity of amino acid sequences and spatial structures of these photoproteins. Based on studies of obelin and aequorin mutants with substitution of Phe to Tyr and Tyr to Phe, respectively [Stepanyuk GA et al. (2005) FEBS Lett 579, 1008-1014], it was suggested that the spectral differences may be accounted for by an additional hydrogen bond between the hydroxyl group of a Tyr residue and an oxygen atom of the 6-(p-hydroxyphenyl) substituent of coelenterazine. Here, we report the crystal structures of two conformation states of the F88Y obelin mutant that has bioluminescence and product fluorescence spectra resembling those of aequorin. Comparison of spatial structures of the F88Y obelin conformation states with those of wild-type obelin clearly shows that substitution of Phe to Tyr does not affect the overall structures of either F88Y obelin or its product following Ca2+ discharge, compared to the conformation states of wild-type obelin. The hydrogen bond network in F88Y obelin being due to the Tyr substitution clearly supports the suggestion that different hydrogen bond patterns near the oxygen of the 6-(p-hydroxyphenyl) substituent are the basis for spectral modifications between hydromedusan photoproteins. Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins.,Natashin PV, Markova SV, Lee J, Vysotski ES, Liu ZJ FEBS J. 2014 Jan 13. doi: 10.1111/febs.12715. PMID:24418253 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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