{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Caspy I"],"funding":["German-Israeli Foundation for Scientific Research and Development","Israel Science Foundation","NIGMS NIH HHS"],"pagination":["1380"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8660910"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["4(1)"],"pubmed_abstract":["Water molecules play a pivotal functional role in photosynthesis, primarily as the substrate for Photosystem II (PSII). However, their importance and contribution to Photosystem I (PSI) activity remains obscure. Using a high-resolution cryogenic electron microscopy (cryo-EM) PSI structure from a Chlamydomonas reinhardtii temperature-sensitive photoautotrophic PSII mutant (TSP4), a conserved network of water molecules - dating back to cyanobacteria - was uncovered, mainly in the vicinity of the electron transport chain (ETC). The high-resolution structure illustrated that the water molecules served as a ligand in every chlorophyll that was missing a fifth magnesium coordination in the PSI core and in the light-harvesting complexes (LHC). The asymmetric distribution of the water molecules ne"],"journal":["Communications biology"],"pubmed_title":["Dimeric and high-resolution structures of Chlamydomonas Photosystem I from a temperature-sensitive Photosystem II mutant."],"pmcid":["PMC8660910"],"funding_grant_id":["R01 GM129325","569/17","P41 GM103311","G-1483-207/2018"],"pubmed_authors":["Schwartz T","Fadeeva M","Caspy I","Ben-Tal N","Kessel A","Bayro-Kaiser V","Nelson N"],"additional_accession":[]},"is_claimable":false,"name":"Dimeric and high-resolution structures of Chlamydomonas Photosystem I from a temperature-sensitive Photosystem II mutant.","description":"Water molecules play a pivotal functional role in photosynthesis, primarily as the substrate for Photosystem II (PSII). However, their importance and contribution to Photosystem I (PSI) activity remains obscure. Using a high-resolution cryogenic electron microscopy (cryo-EM) PSI structure from a Chlamydomonas reinhardtii temperature-sensitive photoautotrophic PSII mutant (TSP4), a conserved network of water molecules - dating back to cyanobacteria - was uncovered, mainly in the vicinity of the electron transport chain (ETC). The high-resolution structure illustrated that the water molecules served as a ligand in every chlorophyll that was missing a fifth magnesium coordination in the PSI core and in the light-harvesting complexes (LHC). The asymmetric distribution of the water molecules ne","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Dec","modification":"2026-05-31T07:09:13.632Z","creation":"2025-04-04T07:57:23.694Z"},"accession":"S-EPMC8660910","cross_references":{"pubmed":["34887518"],"doi":["10.1038/s42003-021-02911-7"]}}