[{"publication":"Nature Communications","language":[{"iso":"eng"}],"status":"public","article_type":"original","article_processing_charge":"Yes","department":[{"_id":"LeSa"}],"pmid":1,"acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"LifeSc"},{"_id":"ScienComp"}],"volume":17,"year":"2026","day":"17","date_published":"2026-08-17T00:00:00Z","_id":"22750","DOAJ_listed":"1","OA_type":"gold","type":"journal_article","date_updated":"2026-09-07T13:17:53Z","ddc":["570"],"intvolume":"        17","supplementarymaterial":"yes","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","dataavailabilitystatement":"The cryo-EM maps are deposited in the Electron Microscopy Data Bank under accession number EMD- 51100 (inactive dimer), EMD- 51102 (active dimer) and EMD-51101 (semi-active dimer). The models are deposited in the Protein Data Bank under accession numbers 9G6F (inactive dimer), 9G6H (active dimer) and 9G6G (semi-active dimer). Mass spectrometry data was uploaded to MassIVE with accession code MSV000101057. Source data are provided with this paper.","date_created":"2026-08-23T22:01:46Z","quality_controlled":"1","oa":1,"month":"08","article_number":"8433","publication_status":"published","oa_version":"Published Version","author":[{"full_name":"Zhao, Ziyu","last_name":"Zhao","first_name":"Ziyu","id":"a63fe682-9f3a-11ee-bf8c-cfdf919b9850"},{"first_name":"Irene","id":"3ED6AF16-F248-11E8-B48F-1D18A9856A87","last_name":"Vercellino","orcid":"0000-0001-5618-3449","full_name":"Vercellino, Irene"},{"last_name":"Whitelegge","full_name":"Whitelegge, Julian P.","first_name":"Julian P."},{"last_name":"Maghlaoui","full_name":"Maghlaoui, Karim","first_name":"Karim"},{"full_name":"Białek, Wojciech","last_name":"Białek","first_name":"Wojciech"},{"full_name":"Nixon, Peter J.","last_name":"Nixon","first_name":"Peter J."},{"orcid":"0000-0002-0977-7989","full_name":"Sazanov, Leonid A","last_name":"Sazanov","id":"338D39FE-F248-11E8-B48F-1D18A9856A87","first_name":"Leonid A"}],"acknowledgement":"P.J.N. is grateful for the support from the Imperial College Electron Microscopy Center. L.A.S. acknowledges the support from the Scientific Service Units (SSU) of IST Austria: the Electron Microscopy Facility (EMF), the Life Science Facility (LSF) and the IST high-performance computing cluster. P.J.N. is grateful for the support of the Biotechnology & Biological Sciences Research Council (awards BB/I00937X/1, BB/L003260/1 and BB/P00931X/1). L.A.S. is grateful to IST Austria for providing the funding.","tmp":{"image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","short":"CC BY-NC-ND (4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode"},"doi":"10.1038/s41467-026-75324-x","researchdata_availability":"yes","corr_author":"1","OA_place":"publisher","publication_identifier":{"eissn":["2041-1723"]},"publisher":"Springer Nature","title":"Cryo-EM structures of naturally occurring dimeric photosystem II complexes lacking the Mn4CaO5 cluster","citation":{"short":"Z. Zhao, I. Vercellino, J.P. Whitelegge, K. Maghlaoui, W. Białek, P.J. Nixon, L.A. Sazanov, Nature Communications 17 (2026).","ieee":"Z. Zhao <i>et al.</i>, “Cryo-EM structures of naturally occurring dimeric photosystem II complexes lacking the Mn4CaO5 cluster,” <i>Nature Communications</i>, vol. 17. Springer Nature, 2026.","ista":"Zhao Z, Vercellino I, Whitelegge JP, Maghlaoui K, Białek W, Nixon PJ, Sazanov LA. 2026. Cryo-EM structures of naturally occurring dimeric photosystem II complexes lacking the Mn4CaO5 cluster. Nature Communications. 17, 8433.","apa":"Zhao, Z., Vercellino, I., Whitelegge, J. P., Maghlaoui, K., Białek, W., Nixon, P. J., &#38; Sazanov, L. A. (2026). Cryo-EM structures of naturally occurring dimeric photosystem II complexes lacking the Mn4CaO5 cluster. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-026-75324-x\">https://doi.org/10.1038/s41467-026-75324-x</a>","ama":"Zhao Z, Vercellino I, Whitelegge JP, et al. Cryo-EM structures of naturally occurring dimeric photosystem II complexes lacking the Mn4CaO5 cluster. <i>Nature Communications</i>. 2026;17. doi:<a href=\"https://doi.org/10.1038/s41467-026-75324-x\">10.1038/s41467-026-75324-x</a>","mla":"Zhao, Ziyu, et al. “Cryo-EM Structures of Naturally Occurring Dimeric Photosystem II Complexes Lacking the Mn4CaO5 Cluster.” <i>Nature Communications</i>, vol. 17, 8433, Springer Nature, 2026, doi:<a href=\"https://doi.org/10.1038/s41467-026-75324-x\">10.1038/s41467-026-75324-x</a>.","chicago":"Zhao, Ziyu, Irene Vercellino, Julian P. Whitelegge, Karim Maghlaoui, Wojciech Białek, Peter J. Nixon, and Leonid A Sazanov. “Cryo-EM Structures of Naturally Occurring Dimeric Photosystem II Complexes Lacking the Mn4CaO5 Cluster.” <i>Nature Communications</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41467-026-75324-x\">https://doi.org/10.1038/s41467-026-75324-x</a>."},"abstract":[{"lang":"eng","text":"Robust oxygenic photosynthesis requires the efficient assembly and repair of the multi-subunit oxygen-evolving photosystem II (PSII) complex. Previous cryogenic electron microscopy (cryo-EM) structures of PSII assembly/disassembly intermediates have relied on the analysis of deletion mutants or removal of PSII subunits in vitro. Here we report the cryo-EM structures of naturally occurring dimeric PSII intermediates from the cyanobacterium Thermosynechococcus vestitus at a resolution of about 2.2 Å. These intermediates contain inactive dimers lacking the oxygen-evolving complex (OEC) and semi-active dimers with the OEC present in one of the two monomers. Our structural data provide a mechanism for how assembly and disassembly of the Mn4CaO5 cluster is coordinated with the binding and release of the extrinsic proteins: restructuring of the C-terminal tail of D1 subunit during assembly or disassembly of the Mn cluster triggers conformational changes in D2, CP47 and CP43 to drive the binding/release of the extrinsic proteins. A combination of structural and mass spectrometry data also suggests that the inactive PSII complexes may include damaged complexes containing oxidized D1-His332, a monodentate ligand to one of the Mn ions of the OEC."}],"file":[{"content_type":"application/pdf","date_updated":"2026-09-07T13:13:03Z","relation":"main_file","success":1,"creator":"dernst","file_size":3370665,"file_name":"2026_NatureComm_Zhao.pdf","date_created":"2026-09-07T13:13:03Z","access_level":"open_access","checksum":"a820b736585de22bcfa30ebdd25a6dd2","file_id":"22843"}],"has_accepted_license":"1","das_tickbox":"1","file_date_updated":"2026-09-07T13:13:03Z","scopus_import":"1","external_id":{"pmid":["42420307"]}}]