<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Nagao R</submitter><funding>MEXT | Japan Society for the Promotion of Science</funding><funding>Japan Agency for Medical Research and Development</funding><pagination>920</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9938196</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>14(1)</volume><pubmed_abstract>Iron-stress-induced-A proteins (IsiAs) are expressed in cyanobacteria under iron-deficient conditions. The cyanobacterium Anabaena sp. PCC 7120 has four isiA genes; however, their binding property and functional roles in PSI are still missing. We analyzed a cryo-electron microscopy structure of a PSI-IsiA supercomplex isolated from Anabaena grown under an iron-deficient condition. The PSI-IsiA structure contains six IsiA subunits associated with the PsaA side of a PSI core monomer. Three of the six IsiA subunits were identified as IsiA1 and IsiA2. The PSI-IsiA structure lacks a PsaL subunit; instead, a C-terminal domain of IsiA2 occupies the position of PsaL, which inhibits the oligomerization of PSI, leading to the formation of a PSI monomer. Furthermore, excitation-energy transfer from I</pubmed_abstract><journal>Nature communications</journal><pubmed_title>Structure of a monomeric photosystem I core associated with iron-stress-induced-A proteins from Anabaena sp. PCC 7120.</pubmed_title><pmcid>PMC9938196</pmcid><funding_grant_id>JP22H04916</funding_grant_id><funding_grant_id>JP20K06528</funding_grant_id><funding_grant_id>JP20H02914</funding_grant_id><funding_grant_id>JP17H06434</funding_grant_id><funding_grant_id>JP21K19085</funding_grant_id><pubmed_authors>Tsuboshita N</pubmed_authors><pubmed_authors>Suzuki T</pubmed_authors><pubmed_authors>Ueno Y</pubmed_authors><pubmed_authors>Kawakami K</pubmed_authors><pubmed_authors>Shimizu S</pubmed_authors><pubmed_authors>Ehira S</pubmed_authors><pubmed_authors>Dohmae N</pubmed_authors><pubmed_authors>Furutani M</pubmed_authors><pubmed_authors>Nakajima Y</pubmed_authors><pubmed_authors>Akimoto S</pubmed_authors><pubmed_authors>Nagao R</pubmed_authors><pubmed_authors>Kato K</pubmed_authors><pubmed_authors>Shen JR</pubmed_authors><pubmed_authors>Hamaguchi T</pubmed_authors><pubmed_authors>Yonekura K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structure of a monomeric photosystem I core associated with iron-stress-induced-A proteins from Anabaena sp. PCC 7120.</name><description>Iron-stress-induced-A proteins (IsiAs) are expressed in cyanobacteria under iron-deficient conditions. The cyanobacterium Anabaena sp. PCC 7120 has four isiA genes; however, their binding property and functional roles in PSI are still missing. We analyzed a cryo-electron microscopy structure of a PSI-IsiA supercomplex isolated from Anabaena grown under an iron-deficient condition. The PSI-IsiA structure contains six IsiA subunits associated with the PsaA side of a PSI core monomer. Three of the six IsiA subunits were identified as IsiA1 and IsiA2. The PSI-IsiA structure lacks a PsaL subunit; instead, a C-terminal domain of IsiA2 occupies the position of PsaL, which inhibits the oligomerization of PSI, leading to the formation of a PSI monomer. Furthermore, excitation-energy transfer from I</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Feb</publication><modification>2026-05-28T16:36:48.586Z</modification><creation>2024-10-15T05:17:50.209Z</creation></dates><accession>S-EPMC9938196</accession><cross_references><pubmed>36805598</pubmed><doi>10.1038/s41467-023-36504-1</doi></cross_references></HashMap>