1S5L
Architecture of the photosynthetic oxygen evolving center
Summary for 1S5L
| Entry DOI | 10.2210/pdb1s5l/pdb |
| Related | 1FE1 1IZL |
| Descriptor | Photosystem Q(B) protein, Photosystem II reaction center protein K, Photosystem II reaction center L protein, ... (28 entities in total) |
| Functional Keywords | photosystem, photosynthesis, oxygen-evolving, tetra-manganese, membrane |
| Biological source | Thermosynechococcus elongatus More |
| Cellular location | Cellular thylakoid membrane; Multi-pass membrane protein: P0A444 Q8DHJ2 Cellular thylakoid membrane; Single-pass membrane protein: Q9F1K9 Q8DIN8 Q8DHA7 Q8DIQ0 Q8DIP0 Q8DIN9 Q8DJ43 Q8DJZ6 Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side: Q9F1L5 P0A386 Cellular thylakoid membrane; Single-pass membrane protein (By similarity): Q9F1R6 P59087 Cellular thylakoid membrane; Multi-pass membrane protein (By similarity): Q8CM25 |
| Total number of polymer chains | 38 |
| Total formula weight | 692749.53 |
| Authors | Ferreira, K.N.,Iverson, T.M.,Maghlaoui, K.,Barber, J.,Iwata, S. (deposition date: 2004-01-21, release date: 2004-02-24, Last modification date: 2024-12-25) |
| Primary citation | Ferreira, K.N.,Iverson, T.M.,Maghlaoui, K.,Barber, J.,Iwata, S. Architecture of the Photosynthetic Oxygen-Evolving Center Science, 303:1831-1838, 2004 Cited by PubMed Abstract: Photosynthesis uses light energy to drive the oxidation of water at an oxygen-evolving catalytic site within photosystem II (PSII). We report the structure of PSII of the cyanobacterium Thermosynechococcus elongatus at 3.5 angstrom resolution. We have assigned most of the amino acid residues of this 650-kilodalton dimeric multisubunit complex and refined the structure to reveal its molecular architecture. Consequently, we are able to describe details of the binding sites for cofactors and propose a structure of the oxygen-evolving center (OEC). The data strongly suggest that the OEC contains a cubane-like Mn3CaO4 cluster linked to a fourth Mn by a mono-micro-oxo bridge. The details of the surrounding coordination sphere of the metal cluster and the implications for a possible oxygen-evolving mechanism are discussed. PubMed: 14764885DOI: 10.1126/science.1093087 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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