4as8

X-ray structure of the cyan fluorescent protein Cerulean cryoprotected with ethylene glycol

spinqualitylabelsall models 4as8, resolution 1.02Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4as8 is a 1 chain structure with sequence from Aeqvi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, MG NonStd Res: CRF Related: 1b9c, 1bfp, 1c4f, 1cv7, 1ema, 1emb, 1emc, 1eme, 1emf, 1emg, 1emk, 1eml, 1emm, 1f09, 1f0b, 1gfl, 1h6r, 1hcj, 1huy, 1jby, 1jbz, 1jc0, 1jc1, 1kp5, 1kyp, 1kyr, 1kys, 1myw, 1q4a, 1q4b, 1q4c, 1q4d, 1q4e, 1q73, 1qxt, 1qy3, 1qyf, 1qyo, 1qyq, 1rm9, 1rmm, 1rmo, 1rmp, 1rrx, 1w7s, 1w7t, 1w7u, 1yfp, 1yhg, 1yhh, 1yhi, 1yj2, 1yjf, 1z1p, 1z1q, 2ah8, 2aha, 2b3p, 2b3q, 2emd, 2emn, 2emo, 2fwq, 2fzu, 2wsn, 2wso, 2wur, 2y0g, 2ydz, 2ye0, 2ye1, 2yfp, 3ztf, 4anj, 4ar7, 4b5y Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. Publication Abstract from PubMed Cryoprotection of a protein crystal by addition of small-molecule compounds may sometimes affect the structure of its active site. The spectroscopic and structural effects of the two cryoprotectants glycerol and ethylene glycol on the cyan fluorescent protein Cerulean were investigated. While glycerol had almost no noticeable effect, ethylene glycol was shown to induce a systematic red shift of the UV-vis absorption and fluorescence emission spectra. Additionally, ethylene glycol molecules were shown to enter the core of the protein, with one of them binding in close vicinity to the chromophore, which provides a sound explanation for the observed spectroscopic changes. These results highlight the need to systematically record spectroscopic data on crystals of light-absorbing proteins and reinforce the notion that fluorescent proteins must not been seen as rigid structures. Alteration of fluorescent protein spectroscopic properties upon cryoprotection.,von Stetten D, Batot GO, Noirclerc-Savoye M, Royant A Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1578-83. doi:, 10.1107/S0907444912037900. Epub 2012 Oct 18. PMID:23090407 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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