3rh8 | pdb_00003rh8

Crystal Structure of the Light-state Dimer of Fungal Blue-Light Photoreceptor Vivid

spinqualitylabelsall models 3rh8, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rh8 is a 2 chain structure with sequence from Neurospora crassa. The March 2015 RCSB PDB Molecule of the Month feature on Phototropin by David Goodsell is 10.2210/rcsb_pdb/mom_2015_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.75Å Ligands: FAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9C3Y6_NEUCS Publication Abstract from PubMed Light, oxygen, or voltage (LOV) protein domains are present in many signaling proteins in bacteria, archaea, protists, plants, and fungi. The LOV protein VIVID (VVD) of the filamentous fungus Neurospora crassa enables the organism to adapt to constant or increasing amounts of light and facilitates proper entrainment of circadian rhythms. Here, we determined the crystal structure of the fully light-adapted VVD dimer and reveal the mechanism by which light-driven conformational change alters the oligomeric state of the protein. Light-induced formation of a cysteinyl-flavin adduct generated a new hydrogen bond network that released the amino (N) terminus from the protein core and restructured an acceptor pocket for binding of the N terminus on the opposite subunit of the dimer. Substitution of residues critical for the switch between the monomeric and the dimeric states of the protein had profound effects on light adaptation in Neurospora. The mechanism of dimerization of VVD provides molecular details that explain how members of a large family of photoreceptors convert light responses to alterations in protein-protein interactions. Structure of a Light-Activated LOV Protein Dimer That Regulates Transcription.,Vaidya AT, Chen CH, Dunlap JC, Loros JJ, Crane BR Sci Signal. 2011 Aug 2;4(184):ra50. PMID:21868352 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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