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/ Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion. Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion. The Journal of biological chemistry 2011 imex curation Tang H., Rothery RA., Voss JE., Weiner JH. Identification is only by mol. wt. but this group have published about 30 detailed biochemical papers over 20 years based on theis purified complex, but this is the only place where they show the actual purification. A&B are identified by western in a related paper (also curated). The dmsABC proteins were introduced into the cell on a plasmid containing the entire dmsABC operon. Triton X-100 E.coli membrane extracts were cleared by centrifugation then applied to a DE-52 column and extracted by salt gradient. Active fractions were further purified by Sephacryl S-300 HR column chromatography. jweiner@ualberta.ca 19-Jan-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation ecoli Escherichia coli (strain K12) ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom weight by comassie molecular weight estimation by coomasie staining weight by comassie Tang H., Rothery RA., Voss JE., Weiner JH. The presence in dmsA and dmsB in the complex purified using this methodology was confirmed by western blotting in PMID:1917829 Identification is only by mol. wt. but this group have published about 30 detailed biochemical papers over 20 years based on theis purified complex, but this is the only place where they show the actual purification. A&B are identified by western in a related paper (also curated). The dmsABC proteins were introduced into the cell on a plasmid containing the entire dmsABC operon. Triton X-100 E.coli membrane extracts were cleared by centrifugation then applied to a DE-52 column and extracted by salt gradient. Active fractions were further purified by Sephacryl S-300 HR column chromatography. jweiner@ualberta.ca Accepted 2015-DEC-22 AT 09:46 GMT AT 09:46 GMT by MGT The Journal of biological chemistry 2011 Only protein-protein interactions imex curation imex curation dmsb_ecoli Anaerobic dimethyl sulfoxide reductase chain B DMSO reductase iron-sulfur subunit dmsB b0895 JW0878 protein protein ecoli Escherichia coli (strain K12) MTTQYGFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQEDNGVWHQNVFAYYLSISCNHCEDPACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRKKHGDLAAVAPLPRAHFTKPNIVIKPNANSRPTGDTTGYLANPKEV 7EC4417EED0809C6 dmsa_ecoli Dimethyl sulfoxide reductase DmsA dmsA b0894 JW5118 protein protein ecoli Escherichia coli (strain K12) MKTKIPDAVLAAEVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVNCGSRCPLRMHVVDGEIKYVETDNTGDDNYDGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGTGTLGGTMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGGVTYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEKTLPASAPKNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWNYAGNCLINQHSEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPSGKIEIYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAACRQEMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPDAKRVDKGGCINVLTTQRPSPLAKGNPSHTNLVQVEKV DIP protein P18775 original sequence version: 96 B97C830ABAC7C32C dmsc_ecoli Anaerobic dimethyl sulfoxide reductase chain C dmsC DMSO reductase anchor subunit JW0879 b0896 protein protein ecoli Escherichia coli (strain K12) MGSGWHEWPLMIFTVFGQCVAGGFIVLALALLKGDLRAEAQQRVIACMFGLWVLMGIGFIASMLHLGSPMRAFNSLNRVGASALSNEIASGSIFFAVGGIGWLLAMLKKLSPALRTLWLIVTMVLGVIFVWMMVRVYNSIDTVPTWYSIWTPMGFFLTMFMGGPLLGYLLLSLAGVDGWAMRLLPAISVLALVVSGVVSVMQGAELATIHSSVQQAAALVPDYGALMSWRIVLLAVALCLWIAPQLKGYQPAVPLLSVSFILLLAGELIGRGVFYGLHMTVGMAVAS DB6D26ACD2BE0CEB dmsa-dmsb-2 1 4 unspecified role unspecified role neutral component neutral component 2 unspecified role unspecified role neutral component neutral component 3 unspecified role unspecified role neutral component neutral component physical association physical association Fig. 4A