5MX2
Photosystem II depleted of the Mn4CaO5 cluster at 2.55 A resolution
Summary for 5MX2
Entry DOI | 10.2210/pdb5mx2/pdb |
Descriptor | Photosystem II protein D1 1, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (35 entities in total) |
Functional Keywords | photosynthesis, metal cluster, edta, hydroxylamine, oxidoreductase, thermosynechococcus elongatus |
Biological source | Thermosynechococcus vestitus BP-1 More |
Total number of polymer chains | 40 |
Total formula weight | 756817.78 |
Authors | Zhang, M.,Bommer, M.,Chatterjee, R.,Hussain, R.,Kern, J.,Yano, J.,Dau, H.,Dobbek, H.,Zouni, A. (deposition date: 2017-01-20, release date: 2017-08-02, Last modification date: 2024-10-09) |
Primary citation | Zhang, M.,Bommer, M.,Chatterjee, R.,Hussein, R.,Yano, J.,Dau, H.,Kern, J.,Dobbek, H.,Zouni, A. Structural insights into the light-driven auto-assembly process of the water-oxidizing Mn4CaO5-cluster in photosystem II. Elife, 6:-, 2017 Cited by PubMed Abstract: In plants, algae and cyanobacteria, Photosystem II (PSII) catalyzes the light-driven splitting of water at a protein-bound MnCaO-cluster, the water-oxidizing complex (WOC). In the photosynthetic organisms, the light-driven formation of the WOC from dissolved metal ions is a key process because it is essential in both initial activation and continuous repair of PSII. Structural information is required for understanding of this chaperone-free metal-cluster assembly. For the first time, we obtained a structure of PSII from without the MnCaO-cluster. Surprisingly, cluster-removal leaves the positions of all coordinating amino acid residues and most nearby water molecules largely unaffected, resulting in a pre-organized ligand shell for kinetically competent and error-free photo-assembly of the MnCaO-cluster. First experiments initiating (i) partial disassembly and (ii) partial re-assembly after complete depletion of the MnCaO-cluster agree with a specific bi-manganese cluster, likely a di-µ-oxo bridged pair of Mn(III) ions, as an assembly intermediate. PubMed: 28718766DOI: 10.7554/eLife.26933 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.197 Å) |
Structure validation
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