8PM1
Structure of Chloroflexus aggregans flavin based fluorescent protein (CagFbFP) variant I52V A85Q
Summary for 8PM1
| Entry DOI | 10.2210/pdb8pm1/pdb |
| Related | 8PKY |
| Descriptor | histidine kinase, FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | lov domain, fluorescent protein |
| Biological source | Chloroflexus aggregans |
| Total number of polymer chains | 2 |
| Total formula weight | 25800.50 |
| Authors | Nikolaev, A.,Remeeva, A.,Gushchin, I. (deposition date: 2023-06-27, release date: 2023-07-05, Last modification date: 2024-01-17) |
| Primary citation | Nikolaev, A.,Tropina, E.V.,Boldyrev, K.N.,Maksimov, E.G.,Borshchevskiy, V.,Mishin, A.,Yudenko, A.,Kuzmin, A.,Kuznetsova, E.,Semenov, O.,Remeeva, A.,Gushchin, I. Two distinct mechanisms of flavoprotein spectral tuning revealed by low-temperature and time-dependent spectroscopy. Protein Sci., 33:e4851-e4851, 2024 Cited by PubMed Abstract: Flavins such as flavin mononucleotide or flavin adenine dinucleotide are bound by diverse proteins, yet have very similar spectra when in the oxidized state. Recently, we developed new variants of flavin-binding protein CagFbFP exhibiting notable blue (Q148V) or red (I52V A85Q) shifts of fluorescence emission maxima. Here, we use time-resolved and low-temperature spectroscopy to show that whereas the chromophore environment is static in Q148V, an additional protein-flavin hydrogen bond is formed upon photoexcitation in the I52V A85Q variant. Consequently, in Q148V, excitation, emission, and phosphorescence spectra are shifted, whereas in I52V A85Q, excitation and low-temperature phosphorescence spectra are relatively unchanged, while emission spectrum is altered. We also determine the x-ray structures of the two variants to reveal the flavin environment and complement the spectroscopy data. Our findings illustrate two distinct color-tuning mechanisms of flavin-binding proteins and could be helpful for the engineering of new variants with improved optical properties. PubMed: 38038877DOI: 10.1002/pro.4851 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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