1GSV
Crystal structure of the P65 crystal form of photoactive yellow protein G47S mutant
Summary for 1GSV
| Entry DOI | 10.2210/pdb1gsv/pdb |
| Related | 1D7E 1F98 1F9I 1GSW 1GSX 2PHY 2PYP 2PYR 3PHY 3PYP |
| Descriptor | PHOTOACTIVE YELLOW PROTEIN, 4'-HYDROXYCINNAMIC ACID (3 entities in total) |
| Functional Keywords | photosynthesis, photoreceptor |
| Biological source | ECTOTHIORHODOSPIRA HALOPHILA |
| Total number of polymer chains | 1 |
| Total formula weight | 14082.76 |
| Authors | Van Aalten, D.M.F.,Crielaard, W.,Hellingwerf, K.J.,Joshua-Tor, L. (deposition date: 2002-01-08, release date: 2002-02-14, Last modification date: 2023-12-13) |
| Primary citation | Van Aalten, D.M.F.,Haker, A.,Hendriks, J.,Hellingwerf, K.J.,Joshua-Tor, L.,Crielaard, W. Engineering Photocycle Dynamics: Crystal Structures and Kinetics of Three Photoactive Yellow Protein Hinge-Bending Mutants J.Biol.Chem., 227:6438-, 2002 Cited by PubMed Abstract: Crystallographic and spectroscopic analyses of three hinge-bending mutants of the photoactive yellow protein are described. Previous studies have identified Gly(47) and Gly(51) as possible hinge points in the structure of the protein, allowing backbone segments around the chromophore to undergo large concerted motions. We have designed, crystallized, and solved the structures of three mutants: G47S, G51S, and G47S/G51S. The protein dynamics of these mutants are significantly affected. Transitions in the photocycle, measured with laser induced transient absorption spectroscopy, show rates up to 6-fold different from the wild type protein and show an additive effect in the double mutant. Compared with the native structure, no significant conformational differences were observed in the structures of the mutant proteins. We conclude that the structural and dynamic integrity of the region around these mutations is of crucial importance to the photocycle and suggest that the hinge-bending properties of Gly(51) may also play a role in PAS domain proteins where it is one of the few conserved residues. PubMed: 11714713DOI: 10.1074/JBC.M109313200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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