DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Nature 2010 imex curation Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. DIP original experiment: DIP-219422X Nature 2010 IMEx Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Nature 2010 imex curation Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. DIP original experiment: DIP-219421X Nature 2010 IMEx Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Nature 2010 imex curation Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. DIP original experiment: DIP-219415X Nature 2010 IMEx Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Nature 2010 imex curation Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. DIP original experiment: DIP-219414X Nature 2010 IMEx Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Nature 2010 imex curation Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. DIP original experiment: DIP-219418X Nature 2010 IMEx Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Nature 2010 imex curation Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. DIP original experiment: DIP-219417X Nature 2010 IMEx Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Nature 2010 imex curation Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. DIP original experiment: DIP-219416X Nature 2010 IMEx Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Nature 2010 imex curation Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. DIP original experiment: DIP-219420X Nature 2010 IMEx Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. Nature 2010 imex curation Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. Only protein-protein interactions ecolx Escherichia coli electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Huang CS., Sadre-Bazzaz K., Shen Y., Deng B., Zhou ZH., Tong L. DIP original experiment: DIP-219419X Nature 2010 IMEx Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase. pccb_human Propionyl-CoA carboxylase beta chain, mitochondrial PCCB Propanoyl-CoA:carbon dioxide ligase subunit beta protein protein human Homo sapiens Human MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHKRGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVPELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPKVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVEAAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL DIP protein P05166 original sequence version: 107 A2DAAC00312D3C0F q5lug0_ruepo pccB SPO1094 protein protein ruepo Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) Silicibacter pomeroyi MKDILSELETRREAARLGGGQKRIDAQHARGKLTARERIELLLDEDSFEEFDMFVSHRCTDFGMEKQRPAGDGVVTGWGTINGRMVYVFSQDFTVFGGSLSETHAQKICKIMDMAVQNGAPVIGINDSGGARIQEGVASLAGYAEVFQRNIMASGVVPQISVIMGPCAGGAVYSPAMTDFIFMVKDTSYMFVTGPDVVKTVTNEVVTAEELGGASTHTRKSSVADGAFENDVEALAEVRRLVDFLPLNNREKPPVRPFFDEPGRIEASLDTLVPENANTPYDMKELINKIADEGDFYEIQEDFAKNIITGFIRLEGQTVGVVANQPMILAGCLDIDSSRKAARFVRFCDCFEIPILTLVDVPGFLPGTSQEYGGVIKHGAKLLFAYGEATVPKVTVITRKAYGGAYDVMASKHLRGDFNYAWPTAEIAVMGAKGATEIIHRADLGDADKIAAHTKDYEGRFANPFVAAERGFIDEVIQPRSTRKRVSRAFASLRGKSLKNPWKKHDNIPL 070AEAE549EB9D37 pccb_rosdo Propionyl-CoA carboxylase beta chain pccB RD1_2028 protein protein rosdo Roseobacter denitrificans (strain ATCC 33942 / OCh 114) MKDILEQLEDRRAAARLGGGQKRIDAQHGRGKLTARERVDLLLDEGSFEEFDMFVTHRCTDFNMQDQKPAGDGVVTGWGTINGRVVYVFSQDFTVLGGSVSETHSKKICKIMDMAMQNGAPVIGINDSGGARIQEGVDSLAGYGEVFQRNIMASGVVPQISMIMGPCAGGAVYSPAMTDFIFMVKDSSYMFVTGPDVVKTVTNEQVSAEELGGATTHTRKSSVADAAFENDVEALAEVRRLVDFLPLNNREKPPVRPFFDDPDRIEPSLDTLVPDNPNTPYDMKELIHKLADEGDFYEIQEEFAKNIITGFIRLEGRTVGVVANQPLVLAGCLDIDSSRKAARFVRFCDAFEIPLLTLIDVPGFLPGTSQEYGGVIKHGAKLLYAYGEATVPMVTVITRKAYGGAYVVMSSKHLRADFNYAWPTAEVAVMGAKGATEIIHRGDLGDPEKIAQHTADYEERFANPFVASERGFVDEVIQPRSTRKRVARAFASLRNKSVQMPWKKHDNIPL DIP protein Q168G2 original sequence version: 26 693077B43EE98CBF pcca_human Propionyl-CoA carboxylase alpha chain, mitochondrial PCCA Propanoyl-CoA:carbon dioxide ligase subunit alpha protein protein human Homo sapiens Human MAGFWVGTAPLVAAGRRGRWPPQQLMLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNEKTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPLHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGFKGHMLTKSEKNQLLAIASSLFVAFQLRAQHFQENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLSVSVDGTQRTVQCLSREAGGNMSIQFLGTVYKVNILTRLAAELNKFMLEKVTEDTSSVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE DIP protein P05165 original sequence version: 128 065F64186A0B8CCC pcca_ruepo Propionyl-CoA carboxylase alpha chain pccA SPO1101 protein protein ruepo Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) Silicibacter pomeroyi MFNKILIANRGEIACRVIKTARKMGISTVAIYSDADKQALHVQMADEAVHIGPPPANQSYIVIDKVMAAIRATGAQAVHPGYGFLSENSKFAEALEAEGVIFVGPPKGAIEAMGDKITSKKIAQEANVSTVPGYMGLIEDADEAVKISNQIGYPVMIKASAGGGGKGMRIAWNDQEAREGFQSSKNEAANSFGDDRIFIEKFVTQPRHIEIQVLCDSHGNGIYLGERECSIQRRNQKVVEEAPSPFLDEATRRAMGEQAVALAKAVGYASAGTVEFIVDGQKNFYFLEMNTRLQVEHPVTELITGVDLVEQMIRVAAGEPLSITQGDVKLTGWAIENRLYAEDPYRGFLPSIGRLTRYRPPAETAAGPLLVNGKWQGDAPSGEAAVRNDTGVYEGGEISMYYDPMIAKLCTWAPTRAAAIEAMRIALDSFEVEGIGHNLPFLSAVMDHPKFISGDMTTAFIAEEYPEGFEGVNLPETDLRRVAAAAAAMHRVAEIRRTRVSGRMDNHERRVGTEWVVTLQGADFPVTIAADHDGSTVSFDDGSSMRVTSDWTPGDQLANLMVDGAPLVLKVGKISGGFRIRTRGADLKVHVRTPRQAELARLMPEKLPPDTSKMLLCPMPGLIVKVDVEVGQEVQEGQALCTIEAMKMENILRAEKKGVVAKINASAGNSLAVDDVIMEFE E9621118EF90D008 E9621118EF90D008 pccb-rppcc_alpha-1 4 12 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 14 unspecified role unspecified role prey prey ecolx Escherichia coli physical association physical association pcca-pccb-1 9 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pccb-pcca-1 6 10 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 13 unspecified role unspecified role prey prey ecolx Escherichia coli physical association physical association rppcc_beta-rppcc_alpha-1 8 11 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 14 unspecified role unspecified role prey prey ecolx Escherichia coli physical association physical association rppcc_alpha-rppcc_beta-1 1 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pccb-rppcc_alpha-2 3 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pcca-pccb-2 5 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 13 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction rppcc_alpha-rppcc_beta-2 2 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pccb-rppcc_alpha-3 7 12 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 14 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction