2ydz | pdb_00002ydz

X-ray structure of the cyan fluorescent protein SCFP3A (K206A mutant)

spinqualitylabelsall models 2ydz, resolution 1.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ydz 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. NonStd Res: CRF Related: 2emn, 1jc0, 2fzu, 1rm9, 1ema, 1rmo, 1f09, 1yhg, 1kp5, 1q73, 1z1p, 2b3q, 1yhh, 1rmm, 1emm, 2b3p, 2fwq, 1emg, 1rmp, 1emb, 2emd, 1q4e, 1q4d, 1kys, 1c4f, 2wur, 1q4a, 1h6r, 1eml, 1w7t, 1emk, 2emo, 2wsn, 1q4b, 1w7u, 1yjf, 1q4c, 1yfp, 1emf, 1yj2, 2ah8, 2wso, 1yhi, 2y0g, 1eme, 1cv7, 1gfl, 1qyq, 2ye1, 2ye0, 1jbz, 1kyr, 2aha, 1rrx, 1qxt, 1myw, 1qy3, 2yfp, 1b9c, 1w7s, 1jby, 3ztf, 1f0b, 1jc1, 1qyo, 1bfp, 1huy, 1hcj, 1emc, 1z1q, 1kyp, 1qyf 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 Cyan variants of green fluorescent protein are widely used as donors in Forster resonance energy transfer experiments. The popular, but modestly bright, Enhanced Cyan Fluorescent Protein (ECFP) was sequentially improved into the brighter variants Super Cyan Fluorescent Protein 3A (SCFP3A) and mTurquoise, the latter exhibiting a high-fluorescence quantum yield and a long mono-exponential fluorescence lifetime. Here we combine X-ray crystallography and excited-state calculations to rationalize these stepwise improvements. The enhancement originates from stabilization of the seventh beta-strand and the strengthening of the sole chromophore-stabilizing hydrogen bond. The structural analysis highlighted one suboptimal internal residue, which was subjected to saturation mutagenesis combined with fluorescence lifetime-based screening. This resulted in mTurquoise2, a brighter variant with faster maturation, high photostability, longer mono-exponential lifetime and the highest quantum yield measured for a monomeric fluorescent protein. Together, these properties make mTurquoise2 the preferable cyan variant of green fluorescent protein for long-term imaging and as donor for Forster resonance energy transfer to a yellow fluorescent protein. Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%.,Goedhart J, von Stetten D, Noirclerc-Savoye M, Lelimousin M, Joosen L, Hink MA, van Weeren L, Gadella TW Jr, Royant A Nat Commun. 2012 Mar 20;3:751. doi: 10.1038/ncomms1738. PMID:22434194 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Green Fluorescent Protein 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA