1R2C
PHOTOSYNTHETIC REACTION CENTER BLASTOCHLORIS VIRIDIS (ATCC)
Summary for 1R2C
| Entry DOI | 10.2210/pdb1r2c/pdb |
| Descriptor | Photosynthetic reaction center cytochrome C subunit precursor, FE (II) ION, SULFATE ION, ... (13 entities in total) |
| Functional Keywords | photosynthetic reaction center, secondary quinone (qb), photosynthesis |
| Biological source | Blastochloris viridis More |
| Cellular location | Cell membrane; Lipid-anchor: P06009 Cellular chromatophore membrane; Multi-pass membrane protein (By similarity): P07173 P06010 Cellular chromatophore membrane; Single-pass membrane protein: P06008 |
| Total number of polymer chains | 4 |
| Total formula weight | 143612.66 |
| Authors | Baxter, R.H.,Ponomarenko, N.,Pahl, R.,Srajer, V.,Moffat, K.,Norris, J.R. (deposition date: 2003-09-26, release date: 2004-04-27, Last modification date: 2024-10-30) |
| Primary citation | Baxter, R.H.,Ponomarenko, N.,Srajer, V.,Pahl, R.,Moffat, K.,Norris, J.R. Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center. Proc.Natl.Acad.Sci.USA, 101:5982-5987, 2004 Cited by PubMed Abstract: Light-induced structural changes in the bacterial reaction center were studied by a time-resolved crystallographic experiment. Crystals of protein from Blastochloris viridis (formerly Rhodopseudomonas viridis) were reconstituted with ubiquinone and analyzed by monochromatic and Laue diffraction, in the dark and 3 ms after illuminating the crystal with a pulsed laser (630 nm, 3 mJ/pulse, 7 ns duration). Refinement of monochromatic data shows that ubiquinone binds only in the "proximal" Q(B) binding site. No significant structural difference was observed between the light and dark datasets; in particular, no quinone motion was detected. This result may be reconciled with previous studies by postulating equilibration of the "distal" and "proximal" binding sites upon extended dark adaption, and in which movement of ubiquinone is not the conformational gate for the first electron transfer between Q(A) and Q(B). PubMed: 15073325DOI: 10.1073/pnas.0306840101 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.86 Å) |
Structure validation
Download full validation report
