5B5E
Crystal structure analysis of Photosystem II complex
Summary for 5B5E
| Entry DOI | 10.2210/pdb5b5e/pdb |
| Related | 5B66 |
| Descriptor | Photosystem II protein D1, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (41 entities in total) |
| Functional Keywords | psii, electron transport, photosynthesis, photosystem, membrane complex, transmembrane alpha-helix, oxygen evolving, water splitting, iron binding, calcium binding, manganese binding, chloride binding, formylation, hydroxylation, thylakoid membrane |
| Biological source | Thermosynechococcus vulcanus More |
| Total number of polymer chains | 38 |
| Total formula weight | 735806.87 |
| Authors | Tanaka, A.,Fukushima, Y.,Kamiya, N. (deposition date: 2016-05-02, release date: 2017-02-01, Last modification date: 2024-11-13) |
| Primary citation | Tanaka, A.,Fukushima, Y.,Kamiya, N. Two Different Structures of the Oxygen-Evolving Complex in the Same Polypeptide Frameworks of Photosystem II J. Am. Chem. Soc., 139:1718-1721, 2017 Cited by PubMed Abstract: The oxygen-evolving complex (OEC) forms the heart of photosystem II (PSII) in photosynthesis. The crystal structure of PSII from Thermosynechococcus vulcanus has been reported at a resolution of 1.9 Å and at an averaged X-ray dose of 0.43 MGy. The OEC structure is suggested to be partially reduced to Mn(II) by EXAFS and DFT computational studies. Recently, the "radiation-damage-free" structures have been published at 1.95 Å resolution using XFEL, but reports continued to appear that the OEC is reduced to the S-state of the Kok cycle. To elucidate much more precise structure of the OEC, in this study two structures were determined at extremely low X-ray doses of 0.03 and 0.12 MGy using conventional synchrotron radiation source. The results indicated that the X-ray reduction effects on the OEC were very small in the low dose region below 0.12 MGy, that is, a threshold existed for the OEC structural changes caused by X-ray exposure. The OEC structures of the two identical monomers in the crystal were clearly different under the threshold of the radiation dose, although the surrounding polypeptide frameworks of PSII were the same. The assumption that the OECs in the crystal were in the dark-stable S-state of the Kok cycle should be re-evaluated. PubMed: 28102667DOI: 10.1021/jacs.6b09666 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
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