8C88
Double mutant G(M19)C/T(L214)C structure of Photosynthetic Reaction Center From Cereibacter sphaeroides strain RV
Summary for 8C88
| Entry DOI | 10.2210/pdb8c88/pdb |
| Descriptor | Reaction center protein H chain, 1,4-DIETHYLENE DIOXIDE, 1,2-ETHANEDIOL, ... (16 entities in total) |
| Functional Keywords | photosynthetic reaction center, bacteriochlorophyll, rhodobacter sphaeroides, spheroidene, ubiquinone, disulfide bond, photosynthesis |
| Biological source | Cereibacter sphaeroides 2.4.1 More |
| Total number of polymer chains | 3 |
| Total formula weight | 101718.71 |
| Authors | Gabdulkhakov, A.,Selikhanov, G.,Fufina, T.,Vasilieva, L.,Atamas, A.,Yukhimchuk, D. (deposition date: 2023-01-19, release date: 2023-11-22, Last modification date: 2024-10-16) |
| Primary citation | Selikhanov, G.,Atamas, A.,Yukhimchuk, D.,Fufina, T.,Vasilieva, L.,Gabdulkhakov, A. Stabilization of Cereibacter sphaeroides Photosynthetic Reaction Center by the Introduction of Disulfide Bonds. Membranes (Basel), 13:-, 2023 Cited by PubMed Abstract: The photosynthetic reaction center of the purple nonsulfur bacterium is a useful model for the study of mechanisms of photoinduced electron transfer and a promising component for photo-bio-electrocatalytic systems. The basic research and technological applications of this membrane pigment-protein complex require effective approaches to increase its structural stability. In this work, a rational design approach to genetically modify the reaction centers by introducing disulfide bonds is used. This resulted in significantly increasing the thermal stability of some of the mutant pigment-protein complexes. The formation of the S-S bonds was confirmed by X-ray crystallography as well as SDS-PAGE, and the optical properties of the reaction centers were studied. The genetically modified reaction centers presented here preserved their ability for photochemical charge separation and could be of interest for basic science and biotechnology. PubMed: 36837657DOI: 10.3390/membranes13020154 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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