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 DksA2, a zinc-independent structural analog of the transcription factor DksA. DksA2, a zinc-independent structural analog of the transcription factor DksA. FEBS Lett. (0014-5793) 2013 Furman R., Biswas T., Danhart EM., Foster MP., Tsodikov OV., Artsimovitch I. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction experimental particp experimental participant identification experimental particp Furman R., Biswas T., Danhart EM., Foster MP., Tsodikov OV., Artsimovitch I. FEBS Lett. (0014-5793) 2013 DksA2, a zinc-independent structural analog of the transcription factor DksA. DksA2, a zinc-independent structural analog of the transcription factor DksA. FEBS Lett. (0014-5793) 2013 Furman R., Biswas T., Danhart EM., Foster MP., Tsodikov OV., Artsimovitch I. in vitro In vitro biochemical biochemical experimental particp experimental participant identification experimental particp Furman R., Biswas T., Danhart EM., Foster MP., Tsodikov OV., Artsimovitch I. FEBS Lett. (0014-5793) 2013 a6vch8_psea7 RNA polymerase-binding transcription factor DksA dksA2 dksA PSPA7_5439 protein protein psea7 Pseudomonas aeruginosa (strain PA7) MSTKAKQQSSQQMTRGFEPYQETKGEEYMSERMRAHFTAILNKWKQELMEEVDRTVHHMQDEAANFPDPADRASQEEEFSLELRARDRERKLIKKIDETLQLIEDEEYGWCDSCGVEIGIRRLEARPTATLCIDCKTLAEIREKQLGS mint 895D7F67E6614FDC rpoc_ecoli DNA-directed RNA polymerase subunit beta' rpoC tabB b3988 JW3951 Transcriptase subunit beta' RNA polymerase subunit beta' protein protein ecoli Escherichia coli (strain K12) MKDLLKFLKAQTKTEEFDAIKIALASPDMIRSWSFGEVKKPETINYRTFKPERDGLFCARIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTQTKVRRERMGHIELASPTAHIWFLKSLPSRIGLLLDMPLRDIERVLYFESYVVIEGGMTNLERQQILTEEQYLDALEEFGDEFDAKMGAEAIQALLKSMDLEQECEQLREELNETNSETKRKKLTKRIKLLEAFVQSGNKPEWMILTVLPVLPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLDLAAPDIIVRNEKRMLQEAVDALLDNGRRGRAITGSNKRPLKSLADMIKGKQGRFRQNLLGKRVDYSGRSVITVGPYLRLHQCGLPKKMALELFKPFIYGKLELRGLATTIKAAKKMVEREEAVVWDILDEVIREHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCAAYNADFDGDQMAVHVPLTLEAQLEARALMMSTNNILSPANGEPIIVPSQDVVLGLYYMTRDCVNAKGEGMVLTGPKEAERLYRSGLASLHARVKVRITEYEKDANGELVAKTSLKDTTVGRAILWMIVPKGLPYSIVNQALGKKAISKMLNTCYRILGLKPTVIFADQIMYTGFAYAARSGASVGIDDMVIPEKKHEIISEAEAEVAEIQEQFQSGLVTAGERYNKVIDIWAAANDRVSKAMMDNLQTETVINRDGQEEKQVSFNSIYMMADSGARGSAAQIRQLAGMRGLMAKPDGSIIETPITANFREGLNVLQYFISTHGARKGLADTALKTANSGYLTRRLVDVAQDLVVTEDDCGTHEGIMMTPVIEGGDVKEPLRDRVLGRVTAEDVLKPGTADILVPRNTLLHEQWCDLLEENSVDAVKVRSVVSCDTDFGVCAHCYGRDLARGHIINKGEAIGVIAAQSIGEPGTQLTMRTFHIGGAASRAAAESSIQVKNKGSIKLSNVKSVVNSSGKLVITSRNTELKLIDEFGRTKESYKVPYGAVLAKGDGEQVAGGETVANWDPHTMPVITEVSGFVRFTDMIDGQTITRQTDELTGLSSLVVLDSAERTAGGKDLRPALKIVDAQGNDVLIPGTDMPAQYFLPGKAIVQLEDGVQISSGDTLARIPQESGGTKDITGGLPRVADLFEARRPKEPAILAEISGIVSFGKETKGKRRLVITPVDGSDPYEEMIPKWRQLNVFEGERVERGDVISDGPEAPHDILRLRGVHAVTRYIVNEVQDVYRLQGVKINDKHIEVIVRQMLRKATIVNAGSSDFLEGEQVEYSRVKIANRELEANGKVGATYSRDLLGITKASLATESFISAASFQETTRVLTEAAVAGKRDELRGLKENVIVGRLIPAGTGYAYHQDRMRRRAAGEAPAAPQVTAEDASASLAELLNAGLGGSDNE DIP protein P0A8T7 original sequence version: 50 DIP protein P0A8T7 original sequence version: 55 DIP protein P0A8T7 original sequence version: 105 DIP protein P0A8T7 original sequence version: 89 A6878C61D15F4961 dksa2 1 DksA2 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 3.0 direct interaction direct interaction mint The coordinates and structure factor amplitudes were deposited in the Protein Data Bank under accession number 4IJJ The crystals contain three molecules of DksA2 per asymmetric unit. This crystallographic trimer is stabilized by three specifically bound sulfate ions from the crystallization solution, with one sulfate coordinating two adjacent DksA2 molecules (Supplementary Fig. S1). t1 st2 sf1 dksa2-rpoc 2 DksA2 3 weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified RNAP 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:44:58 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation disrupting' Arg672Asp undefined mutation mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:44:58 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation disrupting' His673Asp direct interaction direct interaction f2a mint To examine whether, like EC DksA, DksA2 binds in close proximity to the RNAP active site located at the base of the secondary channel, we used Fe2+-mediated cleavage. In this assay, OH radicals generated by Fe2+ ion bound in the RNAP active site cleave nearby protein or nucleic acid regions [5, 15, 16]. We found that the end-labeled DksA2 was cleaved similarly to DksA, and only in the presence of RNAP (Fig. 2A), indicating that DksA2 also binds near the enzyme\'s active site.