6GG9
Crystal structures of a short blue light photoreceptor protein PpSB1-LOV mutant (dark state) - R61H/R66I
Summary for 6GG9
| Entry DOI | 10.2210/pdb6gg9/pdb |
| Descriptor | Sensory box protein, FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | blue light photoreceptor, sensory box protein, signaling protein |
| Biological source | Pseudomonas putida |
| Total number of polymer chains | 4 |
| Total formula weight | 76044.36 |
| Authors | Roellen, K.,Granzin, J.,Batra-Safferling, R. (deposition date: 2018-05-03, release date: 2018-07-25, Last modification date: 2024-01-17) |
| Primary citation | Rollen, K.,Granzin, J.,Batra-Safferling, R.,Stadler, A.M. Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein. PLoS ONE, 13:e0200746-e0200746, 2018 Cited by PubMed Abstract: Light, oxygen, voltage (LOV) photoreceptors consist of conserved photo-responsive domains in bacteria, archaea, plants and fungi, and detect blue-light via a flavin cofactor. We investigated the blue-light induced conformational transition of the dimeric photoreceptor PpSB1-LOV-R66I from Pseudomonas putida in solution by using small-angle X-ray scattering (SAXS). SAXS experiments of the fully populated light- and dark-states under steady-state conditions revealed significant structural differences between the two states that are in agreement with the known structures determined by crystallography. We followed the transition from the light- to the dark-state by using SAXS measurements in real-time. A two-state model based on the light- and dark-state conformations could describe the measured time-course SAXS data with a relaxation time τREC of ~ 34 to 35 min being larger than the recovery time found with UV/vis spectroscopy. Unlike the flavin chromophore-based UV/vis method that is sensitive to the local chromophore environment in flavoproteins, SAXS-based assay depends on protein conformational changes and provides with an alternative to measure the recovery kinetics. PubMed: 30011332DOI: 10.1371/journal.pone.0200746 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.04 Å) |
Structure validation
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