1MPS
PHOTOSYNTHETIC REACTION CENTER MUTANT WITH PHE M 197 REPLACED WITH ARG AND TYR M 177 REPLACED WITH PHE (CHAIN M, Y177F, F197R)
Summary for 1MPS
| Entry DOI | 10.2210/pdb1mps/pdb |
| Descriptor | PHOTOSYNTHETIC REACTION CENTER, LAURYL DIMETHYLAMINE-N-OXIDE, BACTERIOCHLOROPHYLL A, ... (11 entities in total) |
| Functional Keywords | photosynthetic reaction center, transmembrane, electron transport, photosynthesis |
| 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 | 3 |
| Total formula weight | 102390.42 |
| Authors | Mcauley-Hecht, K.E.,Fyfe, P.K.,Ridge, J.P.,Prince, S.,Hunter, C.N.,Isaacs, N.W.,Cogdell, R.J.,Jones, M.R. (deposition date: 1998-03-09, release date: 1998-10-14, Last modification date: 2024-05-22) |
| Primary citation | McAuley-Hecht, K.E.,Fyfe, P.K.,Ridge, J.P.,Prince, S.M.,Hunter, C.N.,Isaacs, N.W.,Cogdell, R.J.,Jones, M.R. Structural studies of wild-type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical properties of the complex from bacterial cell to crystal. Biochemistry, 37:4740-4750, 1998 Cited by PubMed Abstract: Reaction centers have been crystallized from the antenna-deficient RCO2 strain of Rhodobacter sphaeroides, and a structural model has been constructed at 2.6 A resolution. The antenna-deficient strain allows assessment of the structural integrity of the reaction center at each stage in the purification-crystallization procedure. Spectroscopic evidence indicates that the properties of the reaction center bacteriopheophytins and the primary donor bacteriochlorophylls are modified somewhat on removal of the protein complex from the membrane and that these changes are carried through to the crystal form of the reaction center. The structure of a FM197R/YM177F mutant reaction center has also been determined to 2.55 A resolution. The mutant complex shows an unexpected change in structure, with a significant reorientation of the new arginine, the incorporation of a new water molecule into the structure, and rotation of the 2-acetyl carbonyl group of one of the primary donor bacteriochlorophylls to a more out-of-plane geometry. Changes in the optical spectrum of the FM197R/YM177F reaction center are discussed with respect to the altered structure of the complex. PubMed: 9537989DOI: 10.1021/bi971717a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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