DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The molecular origins of specificity in the assembly of a multienzyme complex. The molecular origins of specificity in the assembly of a multienzyme complex. Structure (London, England : 1993) 2005 imex curation Frank RA., Pratap JV., Pei XY., Perham RN., Luisi BF. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Frank RA., Pratap JV., Pei XY., Perham RN., Luisi BF. DIP original experiment: DIP-132823X Structure (London, England : 1993) 2005 IMEx The molecular origins of specificity in the assembly of a multienzyme complex. The molecular origins of specificity in the assembly of a multienzyme complex. The molecular origins of specificity in the assembly of a multienzyme complex. Structure (London, England : 1993) 2005 imex curation Frank RA., Pratap JV., Pei XY., Perham RN., Luisi BF. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Frank RA., Pratap JV., Pei XY., Perham RN., Luisi BF. DIP original experiment: DIP-132821X Structure (London, England : 1993) 2005 IMEx The molecular origins of specificity in the assembly of a multienzyme complex. The molecular origins of specificity in the assembly of a multienzyme complex. The molecular origins of specificity in the assembly of a multienzyme complex. Structure (London, England : 1993) 2005 imex curation Frank RA., Pratap JV., Pei XY., Perham RN., Luisi BF. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Frank RA., Pratap JV., Pei XY., Perham RN., Luisi BF. DIP original experiment: DIP-132822X Structure (London, England : 1993) 2005 IMEx The molecular origins of specificity in the assembly of a multienzyme complex. odp2_geose Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex pdhC E2 Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex protein protein geose Geobacillus stearothermophilus Geobacillus stearothermophilus Bacillus stearothermophilus MAFEFKLPDIGEGIHEGEIVKWFVKPGDEVNEDDVLCEVQNDKAVVEIPSPVKGKVLEILVPEGTVATVGQTLITLDAPGYENMTFKGQEQEEAKKEEKTETVSKEEKVDAVAPNAPAAEAEAGPNRRVIAMPSVRKYAREKGVDIRLVQGTGKNGRVLKEDIDAFLAGGAKPAPAAAEEKAAPAAAKPATTEGEFPETREKMSGIRRAIAKAMVHSKHTAPHVTLMDEADVTKLVAHRKKFKAIAAEKGIKLTFLPYVVKALVSALREYPVLNTSIDDETEEIIQKHYYNIGIAADTDRGLLVPVIKHADRKPIFALAQEINELAEKARDGKLTPGEMKGASCTITNIGSAGGQWFTPVINHPEVAILGIGRIAEKPIVRDGEIVAAPMLALSLSFDHRMIDGATAQKALNHIKRLLSDPELLLMEA DIP protein P11961 original sequence version: 92 DIP protein P11961 original sequence version: 77 DIP protein P11961 original sequence version: 91 DIP protein P11961 original sequence version: 114 2600CD150261ACB0 odpb_geose Pyruvate dehydrogenase E1 component subunit beta pdhB protein protein geose Geobacillus stearothermophilus Geobacillus stearothermophilus Bacillus stearothermophilus MAQMTMVQAITDALRIELKNDPNVLIFGEDVGVNGGVFRATEGLQAEFGEDRVFDTPLAESGIGGLAIGLALQGFRPVPEIQFFGFVYEVMDSICGQMARIRYRTGGRYHMPITIRSPFGGGVHTPELHSDSLEGLVAQQPGLKVVIPSTPYDAKGLLISAIRDNDPVIFLEHLKLYRSFRQEVPEGEYTIPIGKADIKREGKDITIIAYGAMVHESLKAAAELEKEGISAEVVDLRTVQPLDIETIIGSVEKTGRAIVVQEAQRQAGIAANVVAEINERAILSLEAPVLRVAAPDTVYPFAQAESVWLPNFKDVIETAKKVMNF DIP protein P21874 original sequence version: 73 DIP protein P21874 original sequence version: 60 DIP protein P21874 original sequence version: 72 AD1F2D4F82D652AC odpa_geose Pyruvate dehydrogenase E1 component subunit alpha pdhA protein protein geose Geobacillus stearothermophilus Geobacillus stearothermophilus Bacillus stearothermophilus MGVKTFQFPFAEQLEKVAEQFPTFQILNEEGEVVNEEAMPELSDEQLKELMRRMVYTRILDQRSISLNRQGRLGFYAPTAGQEASQIASHFALEKEDFILPGYRDVPQIIWHGLPLYQAFLFSRGHFHGNQIPEGVNVLPPQIIIGAQYIQAAGVALGLKMRGKKAVAITYTGDGGTSQGDFYEGINFAGAFKAPAIFVVQNNRFAISTPVEKQTVAKTLAQKAVAAGIPGIQVDGMDPLAVYAAVKAARERAINGEGPTLIETLCFRYGPHTMSGDDPTRYRSKELENEWAKKDPLVRFRKFLEAKGLWSEEEENNVIEQAKEEIKEAIKKADETPKQKVTDLISIMFEELPFNLKEQYEIYKEKESK DIP protein P21873 original sequence version: 69 DIP protein P21873 original sequence version: 56 DIP protein P21873 original sequence version: 68 DBF43982C0E1926D pdha-pdhb-3 2 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pdha-pdhb-4 1 4 unspecified role unspecified role unspecified role unspecified role Region 122-170 Region 122-170 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association pdha-pdhb-5 3 4 unspecified role unspecified role unspecified role unspecified role Region 122-170 Region 122-170 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association