IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Photosynthesis Research B Floss, G L Igloi, C CassierChauvat, U Muhlenhoff Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species no PMID Cross-linking assays on of photosystem I preparation and purified ferredoxin from Synechococcus elongatus were performed using the cross-linking agent N-ethyl-3-(3-diaminopropyl)carbodiimide (EDC) in the presence ofN-hydroxysulfosuccinimide ester (Sulfo-NHS). fig 4 in vitro In vitro crosslink cross-linking study crosslink western blot western blot Immuno blot Immuno blot B Floss, G L Igloi, C CassierChauvat, U Muhlenhoff Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species no PMID Cross-linking assays on of photosystem I preparation and purified ferredoxin from Synechococcus elongatus were performed using the cross-linking agent N-ethyl-3-(3-diaminopropyl)carbodiimide (EDC) in the presence ofN-hydroxysulfosuccinimide ester (Sulfo-NHS). fig 4 Accepted 2007-NOV-19 by ORCHARD. Photosynthesis Research Photosynthesis Research fer_theeb Ferredoxin-1 Ferredoxin I petF1 petF tsl1009 protein protein theeb Thermosynechococcus elongatus (strain BP-1) MATYKVTLVRPDGSETTIDVPEDEYILDVAEEQGLDLPFSCRAGACSTCAGKLLEGEVDQSDQSFLDDDQIEKGFVLTCVAYPRSDCKILTNQEEELY DE8198FFB127C7AF psad_theeb Photosystem I reaction center subunit II psaD tll1724 Photosystem I 16 kDa polypeptide protein protein theeb Thermosynechococcus elongatus (strain BP-1) MTTLTGQPPLYGGSTGGLLSAADTEEKYAITWTSPKEQVFEMPTAGAAVMREGENLVYFARKEQCLALAAQQLRPRKINDYKIYRIFPDGETVLIHPKDGVFPEKVNKGREAVNSVPRSIGQNPNPSQLKFTGKKPYDP 7073427556CF26F9 petf1-psad-1 1 2 unspecified role unspecified role neutral component neutral component P0A3C9:p.[Glu94Gln;Glu95Gln;Glu96Gln] glu94gln & glu95gln & glu96gln mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E Q certain certain sequence position certain certain certain sequence position certain E Q certain certain sequence position certain certain certain sequence position certain E Q Fri Jul 22 11:06:34 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'glu95gln,glu96gln,glu94gln' Wed May 02 15:16:48 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu94gln,glu95gln,glu96gln' Tue Jun 30 17:45:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Glu94Gln;Glu95Gln;Glu96Gln]' ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role neutral component neutral component synel Synechococcus elongatus direct interaction direct interaction Numbering in original paper refers to mature peptide without the initiator methionine, therefore differs by 1 amino acid Both types of ferredoxins are photoreduced by Photosystem I and can be cross-linked to the PsaD subunit of PS I, although with reduced affinity in case of the E93-95/Q93-95 mutant. The C-terminal acidic patch was found to be important for ferredoxin-mediated electron transfer since the rate of NADP+ photoreduction mediated by the E93-95/Q93-95 mutant ferredoxin accounts for only 25% of the wild-type. Although the E94-96/Q94-96 ferredosin mutant shows a drastic drop of interaction with PsaD, the binding is not completely disrupted indicating another region of the ferredoxin may bind to PsaD.