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 Self-trimerization of ExsD limits inhibition of the Pseudomonas aeruginosa transcriptional activator ExsA in vitro. Self-trimerization of ExsD limits inhibition of the Pseudomonas aeruginosa transcriptional activator ExsA in vitro. FEBS J. (1742-464X) 2013 Bernhards RC., Marsden AE., Esher SK., Yahr TL., Schubot FD. suggested by lperfetto ecoli Escherichia coli (strain K12) complementation protein complementation assay PCA complementation predetermined predetermined participant predetermined Bernhards RC., Marsden AE., Esher SK., Yahr TL., Schubot FD. suggested by lperfetto FEBS J. (1742-464X) 2013 Self-trimerization of ExsD limits inhibition of the Pseudomonas aeruginosa transcriptional activator ExsA in vitro. Self-trimerization of ExsD limits inhibition of the Pseudomonas aeruginosa transcriptional activator ExsA in vitro. FEBS J. (1742-464X) 2013 Bernhards RC., Marsden AE., Esher SK., Yahr TL., Schubot FD. suggested by lperfetto in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column experimental particp experimental participant identification experimental particp Bernhards RC., Marsden AE., Esher SK., Yahr TL., Schubot FD. suggested by lperfetto FEBS J. (1742-464X) 2013 a0a0h2z989_pseab exsD PA14_42380 protein protein pseab Pseudomonas aeruginosa (strain UCBPP-PA14) MEQEDDKQYSREAVFAGRRVSVVGSDARSRGRVPGYASSSLYRESGIISARQLALLQRMLPRLRLEQLFRCEWLQQRLARGLALGREEVRQILLCAAQDDDGWCAELGDRVNLAVPQSMIDWVLLPVYGWWESLLDQAIPGWRLSLVELETQSRQLRIKSEFWSRVAELEPEQAREELARVAKCQARTQEQVAELAGKLETASALAKSAWPNWQRGMATLLASGGLAGFEPIPEVLECLWQPLCRLDDDVGAADAVQAWLHERNLCQAQDHFYWQS mint B63A868DF128C96D exsa_pseae HTH-type transcriptional regulator ExsA exsA PA1713 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MQGAKSLGRKQITSCHWNIPTFEYRVNKEEGVYVLLEGELTVQDIDSTFCLAPGELLFVRRGSYVVSTKGKDSRILWIPLSAQFLQGFVQRFGALLSEVERCDEPVPGIIAFAATPLLAGCVKGLKELLVHEHPPMLACLKIEELLMLFAFSPQGPLLMSVLRQLSNRHVERLQLFMEKHYLNEWKLSDFSREFGMGLTTFKELFGSVYGVSPRAWISERRILYAHQLLLNSDMSIVDIAMEAGFSSQSYFTQSYRRRFGCTPSRSRQGKDECRAKNN 4823D0E9135E0BB7 exsd 2 ExsD 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified A0A0H2Z989:p.Met59Arg mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain M R Tue Jul 12 10:22:32 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 14:25:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'met59arg' Tue Jun 30 18:25:13 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Met59Arg' Stoichiometry: 3.0 direct interaction direct interaction f2b mint With the use of a calibration curve obtained by analyzing a set of standard proteins, we conducted an analytical gel filtration study to estimate the approximate molecular mass of the variant protein. The retention time of the variant protein gave an apparent molecular mass of 42 kDa. While this is somewhat larger than the actual 32 kDa mass of an ExsD monomer, the discrepancy is readily explained by the distinctively non-globular shape of the molecule [30]. In contrast, wild-type ExsD (Fig. 2B) eluted significantly earlier from the gel filtration column and gave an estimated molecular mass of 102 kDa, consistent with a homotrimeric complex as previously reported [30]. exsa-exsa-2 1 ExsA 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ExsA 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association f4 mint Using a bacterial mono-hybrid assay, we were able to demonstrate that ExsDM59R expression efficiently disrupts ExsA dimerization (Fig. 4)