3HJI
1.8 Angstrom Crystal Structure of the I74V:I85V Variant of Vivid (VVD).
Summary for 3HJI
| Entry DOI | 10.2210/pdb3hji/pdb |
| Related | 2pd7 2pd8 2pdT 2pdr 3HJK 3d72 |
| Descriptor | Vivid PAS protein VVD, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | photoreceptor, circadian clock, lov, fad, signaling protein |
| Biological source | Neurospora crassa |
| Total number of polymer chains | 2 |
| Total formula weight | 36541.00 |
| Authors | Zoltowski, B.D.,Vaccaro, B.J.,Crane, B.R. (deposition date: 2009-05-21, release date: 2009-09-29, Last modification date: 2023-09-06) |
| Primary citation | Zoltowski, B.D.,Vaccaro, B.,Crane, B.R. Mechanism-based tuning of a LOV domain photoreceptor. Nat.Chem.Biol., 5:827-834, 2009 Cited by PubMed Abstract: Phototropin-like LOV domains form a cysteinyl-flavin adduct in response to blue light but show considerable variation in output signal and the lifetime of the photo-adduct signaling state. Mechanistic studies of the slow-cycling fungal LOV photoreceptor Vivid (VVD) reveal the importance of reactive cysteine conformation, flavin electronic environment and solvent accessibility for adduct scission and thermal reversion. Proton inventory, pH effects, base catalysis and structural studies implicate flavin N(5) deprotonation as rate-determining for recovery. Substitutions of active site residues Ile74, Ile85, Met135 and Met165 alter photoadduct lifetimes by over four orders of magnitude in VVD, and similar changes in other LOV proteins show analogous effects. Adduct state decay rates also correlate with changes in conformational and oligomeric properties of the protein necessary for signaling. These findings link natural sequence variation of LOV domains to function and provide a means to design broadly reactive light-sensitive probes. PubMed: 19718042DOI: 10.1038/nchembio.210 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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