1AIG
PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE D+QB-CHARGE SEPARATED STATE
Summary for 1AIG
| Entry DOI | 10.2210/pdb1aig/pdb |
| Descriptor | PHOTOSYNTHETIC REACTION CENTER (L SUBUNIT), PHOTOSYNTHETIC REACTION CENTER (M SUBUNIT), PHOTOSYNTHETIC REACTION CENTER (H SUBUNIT), ... (8 entities in total) |
| Functional Keywords | photosynthetic reaction center, integral membrane protein, charge separated |
| Biological source | Rhodobacter sphaeroides More |
| Cellular location | Cellular chromatophore membrane; Multi-pass membrane protein: P02954 P02953 Cellular chromatophore membrane; Single-pass membrane protein: P11846 |
| Total number of polymer chains | 6 |
| Total formula weight | 202178.61 |
| Authors | Stowell, M.H.B.,Mcphillips, T.M.,Soltis, S.M.,Rees, D.C.,Abresch, E.,Feher, G. (deposition date: 1997-04-17, release date: 1997-10-22, Last modification date: 2024-02-07) |
| Primary citation | Stowell, M.H.,McPhillips, T.M.,Rees, D.C.,Soltis, S.M.,Abresch, E.,Feher, G. Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science, 276:812-816, 1997 Cited by PubMed Abstract: High resolution x-ray diffraction data from crystals of the Rhodobacter sphaeroides photosynthetic reaction center (RC) have been collected at cryogenic temperature in the dark and under illumination, and the structures were refined at 2.2 and 2.6 angstrom resolution, respectively. In the charge-separated D+QAQB- state (where D is the primary electron donor (a bacteriochlorophyll dimer), and QA and QB are the primary and secondary quinone acceptors, respectively), QB- is located approximately 5 angstroms from the QB position in the charge-neutral (DQAQB) state, and has undergone a 180 degrees propeller twist around the isoprene chain. A model based on the difference between the two structures is proposed to explain the observed kinetics of electron transfer from QA-QB to QAQB- and the relative binding affinities of the different ubiquinone species in the QB pocket. In addition, several water channels (putative proton pathways) leading from the QB pocket to the surface of the RC were delineated, one of which leads directly to the membrane surface. PubMed: 9115209DOI: 10.1126/science.276.5313.812 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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