1mou Citations

The 2.2 A crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation.

Abstract

Reef-building corals contain host pigments, termed pocilloporins, that function to regulate the light environment of their resident microalgae by acting as a photoprotectant in excessive sunlight. We have determined the crystal structure of an intensely blue, nonfluorescent pocilloporin to 2.2 A resolution and a genetically engineered fluorescent variant to 2.4 A resolution. The pocilloporin chromophore structure adopts a markedly different conformation in comparison with the DsRed chromophore, despite the chromophore sequences (Gln-Tyr-Gly) being identical; the tyrosine ring of the pocilloporin chromophore is noncoplanar and in the trans configuration. Furthermore, the fluorescent variant adopted a noncoplanar chromophore conformation. The data presented here demonstrates that the conformation of the chromophore is highly dependent on its immediate environment.

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  1. Fluorescent proteins as biomarkers and biosensors: throwing color lights on molecular and cellular processes. Stepanenko OV, Verkhusha VV, Kuznetsova IM, Uversky VN, Turoverov KK. Curr Protein Pept Sci 9 338-369 (2008)

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Reviews citing this publication (16)

  1. Fluorescent proteins and their applications in imaging living cells and tissues. Chudakov DM, Matz MV, Lukyanov S, Lukyanov KA. Physiol Rev 90 1103-1163 (2010)
  2. The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins. Verkhusha VV, Lukyanov KA. Nat Biotechnol 22 289-296 (2004)
  3. Fluorescent proteins for live cell imaging: opportunities, limitations, and challenges. Wiedenmann J, Oswald F, Nienhaus GU. IUBMB Life 61 1029-1042 (2009)
  4. GFP family: structural insights into spectral tuning. Pakhomov AA, Martynov VI. Chem Biol 15 755-764 (2008)
  5. Green fluorescent protein: a perspective. Remington SJ. Protein Sci 20 1509-1519 (2011)
  6. Photoconvertible fluorescent protein EosFP: biophysical properties and cell biology applications. Nienhaus GU, Nienhaus K, Hölzle A, Ivanchenko S, Renzi F, Oswald F, Wolff M, Schmitt F, Röcker C, Vallone B, Weidemann W, Heilker R, Nar H, Wiedenmann J. Photochem Photobiol 82 351-358 (2006)
  7. Live-cell imaging with EosFP and other photoactivatable marker proteins of the GFP family. Wiedenmann J, Nienhaus GU. Expert Rev Proteomics 3 361-374 (2006)
  8. Chemical biology-based approaches on fluorescent labeling of proteins in live cells. Jung D, Min K, Jung J, Jang W, Kwon Y. Mol Biosyst 9 862-872 (2013)
  9. Structure, dynamics and optical properties of fluorescent proteins: perspectives for marker development. Nienhaus GU, Wiedenmann J. Chemphyschem 10 1369-1379 (2009)
  10. The role of the protein matrix in green fluorescent protein fluorescence. Maddalo SL, Zimmer M. Photochem Photobiol 82 367-372 (2006)
  11. From EosFP to mIrisFP: structure-based development of advanced photoactivatable marker proteins of the GFP-family. Wiedenmann J, Gayda S, Adam V, Oswald F, Nienhaus K, Bourgeois D, Nienhaus GU. J Biophotonics 4 377-390 (2011)
  12. The kindling fluorescent protein: a transient photoswitchable marker. Henderson JN, Remington SJ. Physiology (Bethesda) 21 162-170 (2006)
  13. The family of GFP-like proteins: structure, function, photophysics and biosensor applications. Introduction and perspective. Wachter RM. Photochem Photobiol 82 339-344 (2006)
  14. Green and red fluorescent proteins: photo- and thermally induced dynamics probed by site-selective spectroscopy and hole burning. Bonsma S, Purchase R, Jezowski S, Gallus J, Könz F, Völker S. Chemphyschem 6 838-849 (2005)
  15. [Chromoproteins of the green fluorescent protein family: properties and applications]. Shkrob M, Mishin AS, Chudakov DM, Labas IuA, Luk'ianov KA. Bioorg Khim 34 581-590 (2008)
  16. Posttranslational chemistry of proteins of the GFP family. Pakhomov AA, Martynov VI. Biochemistry (Mosc) 74 250-259 (2009)

Articles citing this publication (44)