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Exploring chromophore--protein interactions in fluorescent protein cmFP512 from Cerianthus membranaceus: X-ray structure analysis and optical spectroscopy.

Nienhaus K, Renzi F, Vallone B, Wiedenmann J, Nienhaus GU
Biochemistry 45 12942-53 (2006)
Cited: 16 times
EuropePMC logo PMID: 17059211

Abstract

Autofluorescent proteins of the GFP family all share the same three-dimensional beta-can fold; yet they 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 characterization of the green fluorescent protein cmFP512 from Cerianthus membranaceus, a nonbioluminescent, azooxanthellate cnidarian, which has only approximately 22% sequence identity with Aequorea victoria GFP. The X-ray structure, obtained by molecular replacement at a resolution of 1. 35 A, shows the chromophore, formed from the tripeptide Gln-Tyr-Gly, in a hydrogen-bonded cage in the center of an 11-stranded beta-barrel, tightly restrained by adjacent residues and structural water molecules. It exists in a neutral (A) and an anionic (B) species, with absorption/emission maxima at 392/460 (pH 5) and 503/512 nm (pH 7). Their fractional populations and peak positions depend sensitively on pH, reflecting protonation of groups adjacent to the chromophore. The pH dependence of the spectra is explained by a protonation mechanism involving a hydrogen-bonded cluster of charged/polar groups. Cryospectroscopy at 12 K was also performed to analyze the vibronic coupling of the electronic transitions.

Articles - 2c9j mentioned but not cited (2)

  1. A hinge migration mechanism unlocks the evolution of green-to-red photoconversion in GFP-like proteins. Kim H, Zou T, Modi C, Dörner K, Grunkemeyer TJ, Chen L, Fromme R, Matz MV, Ozkan SB, Wachter RM. Structure 23 34-43 (2015)
  2. Structural Consequences of Chromophore Formation and Exploration of Conserved Lid Residues amongst Naturally Occurring Fluorescent Proteins. Zimmer MH, Li B, Shahid RS, Peshkepija P, Zimmer M. Chem Phys 429 5-11 (2014)


Reviews citing this publication (2)

  1. Fluorescent proteins for live cell imaging: opportunities, limitations, and challenges. Wiedenmann J, Oswald F, Nienhaus GU. IUBMB Life 61 1029-1042 (2009)
  2. Fluorescent proteins of the EosFP clade: intriguing marker tools with multiple photoactivation modes for advanced microscopy. Nienhaus K, Nienhaus GU. RSC Chem Biol 2 796-814 (2021)

Articles citing this publication (12)

  1. Structural basis for the phototoxicity of the fluorescent protein KillerRed. Carpentier P, Violot S, Blanchoin L, Bourgeois D. FEBS Lett 583 2839-2842 (2009)
  2. Spectroscopic and structural study of proton and halide ion cooperative binding to gfp. Arosio D, Garau G, Ricci F, Marchetti L, Bizzarri R, Nifosì R, Beltram F. Biophys J 93 232-244 (2007)
  3. Optimized and far-red-emitting variants of fluorescent protein eqFP611. Kredel S, Nienhaus K, Oswald F, Wolff M, Ivanchenko S, Cymer F, Jeromin A, Michel FJ, Spindler KD, Heilker R, Nienhaus GU, Wiedenmann J. Chem Biol 15 224-233 (2008)
  4. Diffusion pathways of oxygen species in the phototoxic fluorescent protein KillerRed. Roy A, Roy A, Carpentier P, Bourgeois D, Field M. Photochem Photobiol Sci 9 1342-1350 (2010)
  5. It's cheap to be colorful. Anthozoans show a slow turnover of GFP-like proteins. Leutenegger A, D'Angelo C, Matz MV, Denzel A, Oswald F, Salih A, Nienhaus GU, Wiedenmann J. FEBS J 274 2496-2505 (2007)
  6. A green fluorescent protein with photoswitchable emission from the deep sea. Vogt A, D'Angelo C, Oswald F, Denzel A, Mazel CH, Matz MV, Ivanchenko S, Nienhaus GU, Wiedenmann J. PLoS One 3 e3766 (2008)
  7. Photophysical Behavior of mNeonGreen, an Evolutionarily Distant Green Fluorescent Protein. Steiert F, Petrov EP, Schultz P, Schwille P, Weidemann T. Biophys J 114 2419-2431 (2018)
  8. Mechanistic insights into reversible photoactivation in proteins of the GFP family. Gayda S, Nienhaus K, Nienhaus GU. Biophys J 103 2521-2531 (2012)
  9. Monomerization of the photoconvertible fluorescent protein SAASoti by rational mutagenesis of single amino acids. Solovyev ID, Gavshina AV, Katti AS, Chizhik AI, Vinokurov LM, Lapshin GD, Ivashina TV, Khrenova MG, Kireev II, Gregor I, Enderlein J, Savitsky AP. Sci Rep 8 15542 (2018)
  10. Axial resolution enhancement by 4Pi confocal fluorescence microscopy with two-photon excitation. Glaschick S, Röcker C, Deuschle K, Wiedenmann J, Oswald F, Mailänder V, Nienhaus GU. J Biol Phys 33 433-443 (2007)
  11. A proton transfer network that generates deprotonated tyrosine is a key to producing reactive oxygen species in phototoxic KillerRed protein. Lee W, Kim I, Rhee YM. Phys Chem Chem Phys 20 22342-22350 (2018)
  12. Ceriantharia (Cnidaria) of the World: an annotated catalogue and key to species. Stampar SN, Reimer JD, Maronna MM, Lopes CSS, Ceriello H, Santos TB, Acuña FH, Morandini AC. Zookeys 952 1-63 (2020)


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