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 Crystal structure of Cu / Zn superoxide dismutase from Taenia solium reveals metal-mediated self-assembly. Crystal structure of Cu / Zn superoxide dismutase from Taenia solium reveals metal-mediated self-assembly. FEBS J. (1742-464X) 2011 Hernández-Santoyo A., Landa A., González-Mondragón E., Pedraza-Escalona M., Parra-Unda R., Rodríguez-Romero A. suggested by lperfetto hersan@servidor.unam.mx in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Hernández-Santoyo A., Landa A., González-Mondragón E., Pedraza-Escalona M., Parra-Unda R., Rodríguez-Romero A. suggested by lperfetto hersan@servidor.unam.mx FEBS J. (1742-464X) 2011 Crystal structure of Cu / Zn superoxide dismutase from Taenia solium reveals metal-mediated self-assembly. Crystal structure of Cu / Zn superoxide dismutase from Taenia solium reveals metal-mediated self-assembly. FEBS J. (1742-464X) 2011 Hernández-Santoyo A., Landa A., González-Mondragón E., Pedraza-Escalona M., Parra-Unda R., Rodríguez-Romero A. suggested by lperfetto hersan@servidor.unam.mx in vitro In vitro ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Hernández-Santoyo A., Landa A., González-Mondragón E., Pedraza-Escalona M., Parra-Unda R., Rodríguez-Romero A. suggested by lperfetto hersan@servidor.unam.mx FEBS J. (1742-464X) 2011 Crystal structure of Cu / Zn superoxide dismutase from Taenia solium reveals metal-mediated self-assembly. Crystal structure of Cu / Zn superoxide dismutase from Taenia solium reveals metal-mediated self-assembly. FEBS J. (1742-464X) 2011 Hernández-Santoyo A., Landa A., González-Mondragón E., Pedraza-Escalona M., Parra-Unda R., Rodríguez-Romero A. suggested by lperfetto hersan@servidor.unam.mx in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Hernández-Santoyo A., Landa A., González-Mondragón E., Pedraza-Escalona M., Parra-Unda R., Rodríguez-Romero A. suggested by lperfetto hersan@servidor.unam.mx FEBS J. (1742-464X) 2011 Crystal structure of Cu / Zn superoxide dismutase from Taenia solium reveals metal-mediated self-assembly. Crystal structure of Cu / Zn superoxide dismutase from Taenia solium reveals metal-mediated self-assembly. FEBS J. (1742-464X) 2011 Hernández-Santoyo A., Landa A., González-Mondragón E., Pedraza-Escalona M., Parra-Unda R., Rodríguez-Romero A. suggested by lperfetto hersan@servidor.unam.mx in vitro In vitro dls dynamic light scattering dls predetermined predetermined participant predetermined Hernández-Santoyo A., Landa A., González-Mondragón E., Pedraza-Escalona M., Parra-Unda R., Rodríguez-Romero A. suggested by lperfetto hersan@servidor.unam.mx FEBS J. (1742-464X) 2011 q8wrf5_taeso Superoxide dismutase [Cu-Zn] CuZnSOD protein protein taeso Taenia solium MKAVCVMRGEEGVKGVVHFTQAGDAVKVHAEFEGLKPGKHGFHVHEFGDTTQGCTSAGAHFNPHGKNHGAPDAAERHVGDLGNVTAGADGKATLDLTDKMISLTGEHSVIGRSLVIHVDPDDLGLGGHELSLITGNAGGRVACGIIGIAKSE mint 0D1DA130373E9B18 cuznsod 3 Cu/Zn SOD 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction mint The atomic coordinates and structure factors have been deposited in the RSCB Protein Data Bank (PDB) with accession number 3MND t1 f3 f4 f5 f7 cuznsod-1 4 Cu/Zn SOD 5 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 mint sf2a sf2b Dynamic light scattering measurements allow us to analyze the aggregation processes in the presence of Zn2+, Cu2+ and Ni2+ ions. As the scattering intensity is proportional to the second power of the particle mass, the contribution to scattering from larger particles dominates the scattering signal [17], as shown in Figure 2S. It was interesting to note that in the Tris buffer pH 8.0, the protein at a concentration of 1 mg/mL is a tetramer. After addition of the ions distinct species appeared in the size distribution extrapolated from the DLS data using the Malvern DTS software. Figure 2S shows the holoenzyme behavior in the presence of different ions. When 1 mM ZnSO4 was added to the DLS cell we observed oligomerization with a peak centered at approximately 300 kDa (Fig. 2SA). If CuSO4 was used, oligomerization was also observed; however, twice the concentration of Cu2+ ions was needed to observe a peak centered at 200 kDa (Fig. 2SB). Conversely, 1 mM NiCl2 produced the opposite effect and the dimeric state was obtained (Fig. 2SC) cuznsod-1 4 Cu/Zn SOD 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction mint sf2c Dynamic light scattering measurements allow us to analyze the aggregation processes in the presence of Zn2+, Cu2+ and Ni2+ ions. As the scattering intensity is proportional to the second power of the particle mass, the contribution to scattering from larger particles dominates the scattering signal [17], as shown in Figure 2S. It was interesting to note that in the Tris buffer pH 8.0, the protein at a concentration of 1 mg/mL is a tetramer. After addition of the ions distinct species appeared in the size distribution extrapolated from the DLS data using the Malvern DTS software. Figure 2S shows the holoenzyme behavior in the presence of different ions. When 1 mM ZnSO4 was added to the DLS cell we observed oligomerization with a peak centered at approximately 300 kDa (Fig. 2SA). If CuSO4 was used, oligomerization was also observed; however, twice the concentration of Cu2+ ions was needed to observe a peak centered at 200 kDa (Fig. 2SB). Conversely, 1 mM NiCl2 produced the opposite effect and the dimeric state was obtained (Fig. 2SC) cuznsod-1 1 Cu/Zn SOD 5 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 sf1b mint Another interesting characteristic of this protein is that its molecular mass distribution changed in the presence of different concentrations of ZnSO4, as determined by gel filtration (Fig. S1). For the pure holoprotein (0.05 mg/mL) in 0.1 M Tris pH 8.5, 0.2 M NaCl and in the absence of ZnSO4 the protein is dimeric. Upon addition of 0.5-1.0 mM ZnSO4 to the protein solution, a new broad peak centred at ~64 kDa appeared at the expense of the dimeric species (32 kDa). cuznsod-1 1 Cu/Zn SOD 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction sf1a mint Another interesting characteristic of this protein is that its molecular mass distribution changed in the presence of different concentrations of ZnSO4, as determined by gel filtration (Fig. S1). For the pure holoprotein (0.05 mg/mL) in 0.1 M Tris pH 8.5, 0.2 M NaCl and in the absence of ZnSO4 the protein is dimeric. Upon addition of 0.5-1.0 mM ZnSO4 tothe protein solution, a new broad peak centred at ~64 kDa appeared at the expense of the dimeric species (32 kDa). cuznsod-1 2 Cu/Zn SOD 5 ms participant Identification by mass spectrometry ms participant predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction f2 mint These results were confirmed by mass spectrometry, which showed several species from monomer to tetramer or even higher molecular weight species, indicating that the protein oligomerizes in the presence of the metal ions (Figure 2).