3LSA
Padron0.9-OFF (non-fluorescent state)
Summary for 3LSA
| Entry DOI | 10.2210/pdb3lsa/pdb |
| Related | 3LS3 |
| Descriptor | Padron0.9, SPERMIDINE, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | beta barrel, cis-trans isomerisation, fluorescent protein |
| Biological source | Pectiniidae |
| Total number of polymer chains | 4 |
| Total formula weight | 109270.89 |
| Authors | Brakemann, T.,Weber, G.,Trowitzsch, S.,Wahl, M.C.,Jakobs, S. (deposition date: 2010-02-12, release date: 2010-03-16, Last modification date: 2024-11-06) |
| Primary citation | Brakemann, T.,Weber, G.,Andresen, M.,Groenhof, G.,Stiel, A.C.,Trowitzsch, S.,Eggeling, C.,Grubmuller, H.,Hell, S.W.,Wahl, M.C.,Jakobs, S. Molecular basis of the light-driven switching of the photochromic fluorescent protein Padron. J.Biol.Chem., 285:14603-14609, 2010 Cited by PubMed Abstract: Reversibly switchable fluorescent proteins can be repeatedly photoswitched between a fluorescent and a nonfluorescent state by irradiation with the light of two different wavelengths. The molecular basis of the switching process remains a controversial topic. Padron0.9 is a reversibly switchable fluorescent protein with "positive" switching characteristics, exhibiting excellent spectroscopic properties. Its chromophore is formed by the amino acids Cys-Tyr-Gly. We obtained high resolution x-ray structures of Padron0.9 in both the fluorescent and the nonfluorescent states and used the structural information for molecular dynamics simulations. We found that in Padron0.9 the chromophore undergoes a cis-trans isomerization upon photoswitching. The molecular dynamics simulations clarified the protonation states of the amino acid residues within the chromophore pocket that influence the protonation state of the chromophore. We conclude that a light driven cis-trans isomerization of the chromophore appears to be the fundamental switching mechanism in all photochromic fluorescent proteins known to date. Distinct absorption cross-sections for the switching wavelengths in the fluorescent and the nonfluorescent state are not essential for efficient photochromism in fluorescent proteins, although they may facilitate the switching process. PubMed: 20236929DOI: 10.1074/jbc.M109.086314 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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