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 The Fe(II)/α-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers. The Fe(II)/α-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers. FEBS J. (1742-464X) 2012 imex curation Knauer SH., Hartl-Spiegelhauer O., Schwarzinger S., Hänzelmann P., Dobbek H. 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 Knauer SH., Hartl-Spiegelhauer O., Schwarzinger S., Hänzelmann P., Dobbek H. FEBS J. (1742-464X) 2012 Only protein-protein interactions imex curation The Fe(II)/α-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers. The Fe(II)/α-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers. FEBS J. (1742-464X) 2012 imex curation Knauer SH., Hartl-Spiegelhauer O., Schwarzinger S., Hänzelmann P., Dobbek H. 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 Knauer SH., Hartl-Spiegelhauer O., Schwarzinger S., Hänzelmann P., Dobbek H. FEBS J. (1742-464X) 2012 Only protein-protein interactions imex curation taud_ecoli Alpha-ketoglutarate-dependent taurine dioxygenase yaiG 2-aminoethanesulfonate dioxygenase tauD ssiD b0368 JW0360 Sulfate starvation-induced protein 3 protein protein ecoli Escherichia coli (strain K12) MSERLSITPLGPYIGAQISGADLTRPLSDNQFEQLYHAVLRHQVVFLRDQAITPQQQRALAQRFGELHIHPVYPHAEGVDEIIVLDTHNDNPPDNDNWHTDVTFIETPPAGAILAAKELPSTGGDTLWTSGIAAYEALSVPFRQLLSGLRAEHDFRKSFPEYKYRKTEEEHQRWREAVAKNPPLLHPVVRTHPVSGKQALFVNEGFTTRIVDVSEKESEALLSFLFAHITKPEFQVRWRWQPNDIAIWDNRVTQHYANADYLPQRRIMHRATILGDKPFYRAG 7ADEB0CDC9CEEB57 taud_psepk Alpha-ketoglutarate-dependent taurine dioxygenase tauD atsK PP_0230 protein protein psepk psepk MSLTITPLSPALGAQISGVDISRDISAEERDAIEQALLQHQVLFLRDQPINPEQQARFAARFGDLHIHPIYPNVPDTPQVLVLDTAVTDVRDNAVWHTDVTFLPTPALGAVLSAKQLPAYGGDTLWASGIAAFEALSAPLREMLDGLTATHDFTKSFPLERFGTTPQDLARWEATRRNNPPLSHPVVRTHPVSGRKALFVNEGFTTRINELSELESDALLRLLFAHATRPEFSIRWRWQENDVAFWDNRVTQHFAVDDYRPNRRVMHRATILGDAPF mint CFA7BB8DDA2DC601 taud-taud 2 tauDpp 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.2 tauDpp 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.2 direct interaction direct interaction mint Oligomeric state of TauDPp. Four molecules were found in the asymmetric unit forming a tetramer (Figure 8A). This arrangement can be described as a dimer of two dimers, one dimer comprising monomers I and III and the other one consisting of monomers II and IV. To investigate if this crystallographic arrangement could be biologically relevant, the tetramer was analyzed using the PISA server. Each monomer exhibits a surface area of 12890 Å2 on average and possible assemblies were tried by inspecting protein interfaces. The results suggest that either a tetramer consisting of monomers I, II, III and IV or a dimer comprising monomers I and III or II and IV, respectively, are stable in solution. The total surface area of the tetramer is 44080 Å2 with 7482 Å2 of buried area whereas the latter is calculated as the difference between the total solvent-accessible surface areas of isolated monomers and the solvent-accessible surface area of the assembly. The dimers have 24590 Å2 and 24280 Å2 as total surface area and 1314 Å2 and 1376 Å2 of buried areas. Dividing the size of the buried area of a dimer by two leads to the interface area per monomer. t1 f8 f9 PDB ID code 3PVJ - 3V17 - 3V15 taud-1 1 tauDpp 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction sf1 sf2 mint investigate the oligomeric state of the native enzymes. The sedimentation coefficient distribution revealed one hydrodynamically distinct species for both enzymes with a molecular mass of 120 ± 2 kDa for TauDPp and 127 ± 4 kDa for TauDEc, which are in excellent agreement with the theoretical molecular mass for the TauDPp tetramer of 124 kDa and 128 kDa for the TauDEc tetramer and clearly corroborate a homotetrameric state of both taurine dioxygenases in solution. taud-1 1 tauDEc 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction sf1 sf2 mint investigate the oligomeric state of the native enzymes. The sedimentation coefficient distribution revealed one hydrodynamically distinct species for both enzymes with a molecular mass of 120 ± 2 kDa for TauDPp and 127 ± 4 kDa for TauDEc, which are in excellent agreement with the theoretical molecular mass for the TauDPp tetramer of 124 kDa and 128 kDa for the TauDEc tetramer and clearly corroborate a homotetrameric state of both taurine dioxygenases in solution.