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 anonymous-2014o-2 Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined rezacova@uochb.cas.cz 2014 imex curation Skerlová J., Fábry M., Hubálek M., Otwinowski Z., Rezáčová P. FEBS J. (1742-464X) Only protein-protein interactions anonymous-2014k-1 Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined rezacova@uochb.cas.cz 2014 imex curation Skerlová J., Fábry M., Hubálek M., Otwinowski Z., Rezáčová P. FEBS J. (1742-464X) Only protein-protein interactions deor_bacsu Deoxyribonucleoside regulator deoR yxxC BSU39430 protein protein bacsu Bacillus subtilis MDREKQQLSIEAARLYYQSDYSQQQIAEQLNISRPTVSRLLQYAKEKGYVQIRVMDPFEDLDALGSILEEKYGLLEAHVVFSPTPDYAGITHDLSRYGAEYMHETVKDGDIVGVSWGTTMYQIAQNMQPKQVKGVEVVQLKGGISHSRVNTYSAETIQLFAEAFQTMPRYLPLPVVFDNADVKRMVEKDRHIERIIEMGKQANIALFTVGTVRDEALLFRLGYFNEEEKALLKKQAVGDICSRFFDAKGNICSSAINDRTIGVELQDLRLKERSILVAGGSRKVSSIHGALTGKYANVLIIDQHTARALVNDL deor-1 1539593 n/a C-DeoR 1539595 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 2.0 direct interaction direct interaction false false false f7 We analysed the oligomeric state of both C-DeoR and full-length DeoR in solution by analytical size-exclusion chromatography. The apparent molecular weight of C-DeR as well as that of the full-length DeoR protein was estimated in the presence or absence of the effector molecule dR5P. These experiments revealed that C-DeoR forms dimers in solution which persist in the presence of dR5P. Full-length DeoR forms tetramers in solution and this oligomeric assembly is also observed in the presence of dR5P (Figure 7). deor-1 1539593 n/a DeoR 1539595 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false f7 We analysed the oligomeric state of both C-DeoR and full-length DeoR in solution by analytical size-exclusion chromatography. The apparent molecular weight of C-DeR as well as that of the full-length DeoR protein was estimated in the presence or absence of the effector molecule dR5P. These experiments revealed that C-DeoR forms dimers in solution which persist in the presence of dR5P. Full-length DeoR forms tetramers in solution and this oligomeric assembly is also observed in the presence of dR5P (Figure 7). deor-1 1539594 n/a C-DeoR 1539595 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 2.0 direct interaction direct interaction false false false t1 f1 f2d f3 f8