4YUU
Crystal structure of oxygen-evolving photosystem II from a red alga
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Summary for 4YUU
| Entry DOI | 10.2210/pdb4yuu/pdb |
| Descriptor | Photosystem II protein D1, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (40 entities in total) |
| Functional Keywords | transmembrane alpha-helix, electron transport, photosynthesis, photosystem ii, water-splitting, oxygen-evolving, iron binding, calcium binding, manganese binding, chloride binding, thylakoid membrane |
| Biological source | Cyanidium caldarium More |
| Total number of polymer chains | 84 |
| Total formula weight | 1579524.08 |
| Authors | Ago, H.,Shen, J.-R. (deposition date: 2015-03-19, release date: 2016-01-20, Last modification date: 2024-11-06) |
| Primary citation | Ago, H.,Adachi, H.,Umena, Y.,Tashiro, T.,Kawakami, K.,Kamiya, N.,Tian, L.,Han, G.,Kuang, T.,Liu, Z.,Wang, F.,Zou, H.,Enami, I.,Miyano, M.,Shen, J.-R. Novel Features of Eukaryotic Photosystem II Revealed by Its Crystal Structure Analysis from a Red Alga J.Biol.Chem., 291:5676-5687, 2016 Cited by PubMed Abstract: Photosystem II (PSII) catalyzes light-induced water splitting, leading to the evolution of molecular oxygen indispensible for life on the earth. The crystal structure of PSII from cyanobacteria has been solved at an atomic level, but the structure of eukaryotic PSII has not been analyzed. Because eukaryotic PSII possesses additional subunits not found in cyanobacterial PSII, it is important to solve the structure of eukaryotic PSII to elucidate their detailed functions, as well as evolutionary relationships. Here we report the structure of PSII from a red alga Cyanidium caldarium at 2.76 Å resolution, which revealed the structure and interaction sites of PsbQ', a unique, fourth extrinsic protein required for stabilizing the oxygen-evolving complex in the lumenal surface of PSII. The PsbQ' subunit was found to be located underneath CP43 in the vicinity of PsbV, and its structure is characterized by a bundle of four up-down helices arranged in a similar way to those of cyanobacterial and higher plant PsbQ, although helices I and II of PsbQ' were kinked relative to its higher plant counterpart because of its interactions with CP43. Furthermore, two novel transmembrane helices were found in the red algal PSII that are not present in cyanobacterial PSII; one of these helices may correspond to PsbW found only in eukaryotic PSII. The present results represent the first crystal structure of PSII from eukaryotic oxygenic organisms, which were discussed in comparison with the structure of cyanobacterial PSII. PubMed: 26757821DOI: 10.1074/jbc.M115.711689 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.77000368116 Å) |
Structure validation
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