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/ Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster. Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster. Science (0036-8075) 2000 Dai S., Schwendtmayer C., Schurmann P., Ramaswamy S., Eklund H. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species The structure of the oxidized FTR was determined by multiplde isomorphous replacement (MIR) with the help of multiwavelength anomalous dispersion (MAD) data collected on the iron edge for the iron-sulfur center. hasse@xray.bmc.uu.se in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Dai S., Schwendtmayer C., Schurmann P., Ramaswamy S., Eklund H. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species The structure of the oxidized FTR was determined by multiplde isomorphous replacement (MIR) with the help of multiwavelength anomalous dispersion (MAD) data collected on the iron edge for the iron-sulfur center. hasse@xray.bmc.uu.se Annotation to indicate that this entry has been checked and accepted by a senior curator. Science (0036-8075) 2000 ftrv_syny3 Ferredoxin-thioredoxin reductase, variable chain ftrV Ferredoxin-thioredoxin reductase subunit A ssr0330 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MNVGDRVRVTSSVVVYHHPEHKKTAFDLQGMEGEVAAVLTEWQGRPISANLPVLVKFEQRFKAHFRPDEVTLIED DIP protein Q55781 original sequence version: 81 37C5E0D41C22C18E ftrc_syny3 Ferredoxin-thioredoxin reductase, catalytic chain ftrC Ferredoxin-thioredoxin reductase subunit B sll0554 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MTSSDTQNNKTLAAMKNFAEQYAKRTDTYFCSDLSVTAVVIEGLARHKEELGSPLCPCRHYEDKEAEVKNTFWNCPCVPMRERKECHCMLFLTPDNDFAGDAQDIPMETLEEVKASMA DIP protein Q55389 original sequence version: 80 93B2F674C59A3CCE ftrv-ftrc-1 1 3 unspecified role unspecified role neutral component neutral component sulfide bond sulfide bond binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 2 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction 1.60A working 23.8%, free 27.8% FTR is an iron-sulfur enzume composed a conserved catalytic subunit and a varaiable subunit. The catalytic subunit contains a redox-active disulfide and a [4fe-4S] center. The interaction between the catalytic and variable chains involves the very thin center of the molecule where only a small hydrophobic core is formed. However, most of the interactions occur between charged and polar residues that form hydrogen bonds. One inmportant function of the variable subunit seems the stablization of the Fe-S cluster of the catalytic subunit. Reduced ferredoxin produced by photosytem I during light is used by this heterodimer enzyme ferredoxin:thioredoxin reductase (FTR) to reduce the sulfide bond of thioredoxins which will the regulates many target enzymes. FTR is key enzyme sensing light-dependent redox potential changes transforming the electron signal to a thiol signal. The active-site disulfide bridge between Cys57 and Cys87 of catalytic subunit is in van der Waals contact with the iron center. This bridge is believed to be disrupted when ferrodoxin gives 1 electron. The Cys57 forms then a disulfid bond with thioredoxin by disrupting an internal disulfide bond in thioredoxin. A second electron given by a new ferrodoxin free the thioredoxin which is then reduced and the cys57 forms again an internal sulfid bond cys 87.