MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint rivera_calzada-2013- Structure of a bacterial type IV secretion core complex at subnanometre resolution. in vitro In vitro affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom edman degradation edman degradation Rivera-Calzada A., Fronzes R., Savva C.G., Chandran V., Lian P.W., Laeremans T., Pardon E., Steyaert J., Remaut H., Waksman G., Orlova E.V. g.waksman@mail.cryst.bbk.ac.uk EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation rivera_calzada-2013- Structure of a bacterial type IV secretion core complex at subnanometre resolution. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Rivera-Calzada A., Fronzes R., Savva C.G., Chandran V., Lian P.W., Laeremans T., Pardon E., Steyaert J., Remaut H., Waksman G., Orlova E.V. g.waksman@mail.cryst.bbk.ac.uk EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation rivera_calzada-2013- Structure of a bacterial type IV secretion core complex at subnanometre resolution. in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Rivera-Calzada A., Fronzes R., Savva C.G., Chandran V., Lian P.W., Laeremans T., Pardon E., Steyaert J., Remaut H., Waksman G., Orlova E.V. g.waksman@mail.cryst.bbk.ac.uk EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation q46705_ecolx traF protein protein ecolx Escherichia coli MARKSVDVDQELDENTGDGEFESERGGFNGSNRRSAPRMKAFVILMALLALVFIGITVMGKIRAPAKAEADKDGGKAQQANTLPNYSFNSDPDVNKPATAQNSPTDARAVQAAAQADADAGSSNTGARTSNKRKEPSPEELAMQRRLGGELAQTNQAATSNSPGAQPQDNETSEGSSALAKNLTPARLKASRAGVMANPSLTVPKGKMIPCGTGTELDTTVPGQVSCRVSQDVYSADGLVRLIDKGSWVDGQITGGIKDGQARVFVLWERIRNDQDGTIVNIDSAGTNSLGSAGIPGQVDAHMWERLAGAIMISLFSDTLTALVNQTQSNNIQYNSTENSGGQLASEALRSYMSIPPTLYDQQGDAVSIFVARDLDFSGVYTLADN 3F94CFD32ED8316B q46702_ecolx traN protein protein ecolx Escherichia coli MRSLLLMGVLLISACSSGHKPPPEPDWSNTVPVNKTIPVDTQGGRNES 43ACC8EA9591FBAB q46704_ecolx traO protein protein ecolx Escherichia coli MKKLLLSAVVLSVLGGAATNVMALEVGRNSPYDYRIKSVVYNPVNVVKIDAVAGVATHIVVAPDETYITHAFGDSESRTFAHKMNHFFVKPKQAMSDTNLVIVTDKRTYNIVLHFIGEETKKNADGTVSKSFIETPWAVRHAVLQLTYEYPFEQQEKAKSAADKKRITQKLKQTAFAGAKNYQYVMSEQPEMRSIQPVHVWDNYRFTRFEFPANAELPQVYMISASGKETLPNSHVVGENRNIIEVETVAKEWRIRLGDKVVGVRNNNFAPGRGAVATGTASPDVRRVQIGEDN DCAE0E16EEB542FC traf-tran-1 1445742 n/a 1445745 unspecified role unspecified role bait bait strep tag strep tag strep tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range false n/a 1445746 unspecified role unspecified role prey prey n/a 1445747 unspecified role unspecified role prey prey physical association physical association false false false f1b Digestion of the FLCC with elastase produced a stable truncated complex of around 880 kDa in molecular weight, termed the ‘CCelastase’ complex (Figure 1). The N-terminal sequencing of the two main bands in SDS-PAGE gels confirms that the complex is made of full-length TraO/VirB9 and the C-terminal domain of TraF/VirB10 starting at N161SPGA (the integrity of the C terminus of TraF/VirB10CTwas confirmed by western blotting analysis of the Strep-tag present at the C terminus of the TraF/ VirB10 construct). Therefore, the IL of this complex is only made of TraO/VirB9NT (Figure 1). The expected molecular weight of a 14-mer for this new truncated complex is B830 kDa, which is very close to the measured molecular weight indicated above traf-trao-1 1445742 n/a 1445747 unspecified role unspecified role prey prey n/a TraF 1445745 unspecified role unspecified role bait bait binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false strep tag strep tag strep tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range false physical association physical association false false false f1b traf-tran-3 1445743 n/a 1445746 unspecified role unspecified role neutral component neutral component n/a 1445747 unspecified role unspecified role neutral component neutral component n/a 1445745 unspecified role unspecified role neutral component neutral component strep tag strep tag strep tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range false physical association physical association false false false f1c Digestion of the FLCC with elastase produced a stable truncated complex of around 880 kDa in molecular weight, termed the ‘CCelastase’ complex (Figure 1). The N-terminal sequencing of the two main bands in SDS-PAGE gels confirms that the complex is made of full-length TraO/VirB9 and the C-terminal domain of TraF/VirB10 starting at N161SPGA (the integrity of the C terminus of TraF/VirB10CTwas confirmed by western blotting analysis of the Strep-tag present at the C terminus of the TraF/ VirB10 construct). Therefore, the IL of this complex is only made of TraO/VirB9NT (Figure 1). The expected molecular weight of a 14-mer for this new truncated complex is B830 kDa, which is very close to the measured molecular weight indicated above traf-trao-2 1445743 n/a 1445747 unspecified role unspecified role neutral component neutral component n/a TraF 1445745 unspecified role unspecified role neutral component neutral component binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false strep tag strep tag strep tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range false direct interaction direct interaction false false false f1c traf-tran-6 1445744 n/a TraO 1445747 unspecified role unspecified role neutral component neutral component Stoichiometry: 14.0 direct interaction direct interaction false false false f2 Digestion of the FLCC with elastase produced a stable truncated complex of around 880 kDa in molecular weight, termed the ‘CCelastase’ complex (Figure 1). The N-terminal sequencing of the two main bands in SDS-PAGE gels confirms that the complex is made of full-length TraO/VirB9 and the C-terminal domain of TraF/VirB10 starting at N161SPGA (the integrity of the C terminus of TraF/VirB10CTwas confirmed by western blotting analysis of the Strep-tag present at the C terminus of the TraF/ VirB10 construct). Therefore, the IL of this complex is only made of TraO/VirB9NT (Figure 1). The expected molecular weight of a 14-mer for this new truncated complex is B830 kDa, which is very close to the measured molecular weight indicated above