1LGH
CRYSTAL STRUCTURE OF THE LIGHT-HARVESTING COMPLEX II (B800-850) FROM RHODOSPIRILLUM MOLISCHIANUM
Summary for 1LGH
| Entry DOI | 10.2210/pdb1lgh/pdb |
| Descriptor | LIGHT HARVESTING COMPLEX II, BACTERIOCHLOROPHYLL A, LYCOPENE, ... (7 entities in total) |
| Functional Keywords | light harvesting complex, bacteriochlorophyll, dexter energy transfer, foerster exciton transfer mechanism, membrane protein, photosynthesis |
| Biological source | Phaeospirillum molischianum More |
| Cellular location | Cell inner membrane; Single-pass type II membrane protein: P97253 P95673 |
| Total number of polymer chains | 8 |
| Total formula weight | 63490.25 |
| Authors | Koepke, J.,Hu, X.,Schulten, K.,Michel, H. (deposition date: 1996-03-20, release date: 1997-06-05, Last modification date: 2024-12-25) |
| Primary citation | Koepke, J.,Hu, X.,Muenke, C.,Schulten, K.,Michel, H. The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum. Structure, 4:581-597, 1996 Cited by PubMed Abstract: The light-harvesting complexes II (LH-2s) are integral membrane proteins that form ring-like structures, oligomers of alpha beta-heterodimers, in the photosynthetic membranes of purple bacteria. They contain a large number of chromophores organized optimally for light absorption and rapid light energy migration. Recently, the structure of the nonameric LH-2 of Rhodopseudomonas acidophila has been determined; we report here the crystal structure of the octameric LH-2 from Rhodospirillum molischianum. The unveiling of similarities and differences in the architecture of these proteins may provide valuable insight into the efficient energy transfer mechanisms of bacterial photosynthesis. PubMed: 8736556DOI: 10.1016/S0969-2126(96)00063-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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