2c9i

STRUCTURE OF THE FLUORESCENT PROTEIN ASFP499 FROM ANEMONIA SULCATA

spinqualitylabelsall models 2c9i, resolution 1.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c9i is a 8 chain structure with sequence from Anemonia sulcata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: CRQ Related: 1b9c, 1bfp, 1c4f, 1ema, 1emb, 1emc, 1eme, 1emf, 1emg, 1emk, 1eml, 1emm, 1f09, 1f0b, 1g7k, 1gfl, 1ggx, 1h6r, 1hcj, 1huy, 1jby, 1jbz, 1jc0, 1jc1, 1kp5, 1kyp, 1kyr, 1kys, 1myw, 1oxd, 1oxe, 1oxf, 1q4a, 1q4b, 1q4c, 1q4d, 1q4e, 1q73, 1qxt, 1qy3, 1qyf, 1rm9, 1rmm, 1rmo, 1rmp, 1rrx, 1s6z, 1w7s, 1w7t, 1w7u, 1xa9, 1xae, 1xss, 1yjf, 1z1p, 1z1q, 1zgo, 1zgp, 1zgq, 1zux, 2a46, 2a50, 2a52, 2a53, 2a54, 2a56, 2b3p, 2b3q, 2btj, 2c9j, 2emd, 2emn, 2emo Resources: FirstGlance, OCA, RCSB, PDBsum 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 Despite their similar fold topologies, anthozoan fluorescent proteins (FPs) can exhibit widely different optical properties, arising either from chemical modification of the chromophore itself or from specific interactions of the chromophore with the surrounding protein moiety. Here we present a structural and spectroscopic investigation of the green FP asFP499 from the sea anemone Anemonia sulcata var. rufescens to explore the effects of the protein environment on the chromophore. The optical absorption and fluorescence spectra reveal two discrete species populated in significant proportions over a wide pH range. Moreover, multiple protonation reactions are evident from the observed pH-dependent spectral changes. The x-ray structure of asFP499, determined by molecular replacement at a resolution of 1.85 A, shows the typical beta-barrel fold of the green FP from Aequorea victoria (avGFP). In its center, the chromophore, formed from the tripeptide Gln(63)-Tyr(64)-Gly(65), is tightly held by multiple hydrogen bonds in a polar cage that is structurally quite dissimilar to that of avGFP. The x-ray structure provides interesting clues as to how the spectroscopic properties are fine tuned by the chromophore environment. Chromophore-protein interactions in the anthozoan green fluorescent protein asFP499.,Nienhaus K, Renzi F, Vallone B, Wiedenmann J, Nienhaus GU Biophys J. 2006 Dec 1;91(11):4210-20. Epub 2006 Sep 15. PMID:16980366 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Green Fluorescent Protein

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