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 Structure and function of BamE within the outer membrane and the β-barrel assembly machine. Structure and function of BamE within the outer membrane and the β-barrel assembly machine. EMBO Rep. (1469-221X) 2011 imex curation Knowles TJ., Browning DF., Jeeves M., Maderbocus R., Rajesh S., Sridhar P., Manoli E., Emery D., Sommer U., Spencer A., Leyton DL., Squire D., Chaudhuri RR., Viant MR., Cunningham AF., Henderson IR., Overduin M. 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 Knowles TJ., Browning DF., Jeeves M., Maderbocus R., Rajesh S., Sridhar P., Manoli E., Emery D., Sommer U., Spencer A., Leyton DL., Squire D., Chaudhuri RR., Viant MR., Cunningham AF., Henderson IR., Overduin M. EMBO Rep. (1469-221X) 2011 Only protein-protein interactions imex curation Structure and function of BamE within the outer membrane and the β-barrel assembly machine. Structure and function of BamE within the outer membrane and the β-barrel assembly machine. EMBO Rep. (1469-221X) 2011 imex curation Knowles TJ., Browning DF., Jeeves M., Maderbocus R., Rajesh S., Sridhar P., Manoli E., Emery D., Sommer U., Spencer A., Leyton DL., Squire D., Chaudhuri RR., Viant MR., Cunningham AF., Henderson IR., Overduin M. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Knowles TJ., Browning DF., Jeeves M., Maderbocus R., Rajesh S., Sridhar P., Manoli E., Emery D., Sommer U., Spencer A., Leyton DL., Squire D., Chaudhuri RR., Viant MR., Cunningham AF., Henderson IR., Overduin M. EMBO Rep. (1469-221X) 2011 Only protein-protein interactions imex curation bame_ecoli Outer membrane protein assembly factor BamE bamE smpA b2617 JW2598 protein protein ecoli Escherichia coli (strain K12) MRCKTLTAAAAVLLMLTAGCSTLERVVYRPDINQGNYLTANDVSKIRVGMTQQQVAYALGTPLMSDPFGTNTWFYVFRQQPGHEGVTQQTLTLTFNSSGVLTNIDNKPALSGN DIP protein P0A937 original sequence version: 75 DIP protein P0A937 original sequence version: 87 DIP protein P0A937 original sequence version: 88 CFD8840C014AA0A2 bamd_ecoli Outer membrane protein assembly factor BamD bamD yfiO JW2577 b2595 protein protein ecoli Escherichia coli (strain K12) MTRMKYLVAAATLSLFLAGCSGSKEEVPDNPPNEIYATAQQKLQDGNWRQAITQLEALDNRYPFGPYSQQVQLDLIYAYYKNADLPLAQAAIDRFIRLNPTHPNIDYVMYMRGLTNMALDDSALQGFFGVDRSDRDPQHARAAFSDFSKLVRGYPNSQYTTDATKRLVFLKDRLAKYEYSVAEYYTERGAWVAVVNRVEGMLRDYPDTQATRDALPLMENAYRQMQMNAQAEKVAKIIAANSSNT DIP protein P0AC02 original sequence version: 70 DIP protein P0AC02 original sequence version: 82 DIP protein P0AC02 original sequence version: 83 91D0A25E69248C49 bamd-bame 2 BamD 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified BamE 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction mint f4 sf9 bame-1 1 BamE 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 2.0 direct interaction direct interaction mint sf1b sf1d whole-cell purification yielded a mixture of monomer and dimer (supplementary Fig S1B online). The different folding outcomes are dictated by the environment; expression at lower temperatures favours periplasmic monomer and at elevated temperatures yields uncleaved cytosolic dimer (supplementary Fig S1C,D online). Analysis of expression levels showed that increasing the temperature prevents export from the cytosol, suggesting that the dimer is a misfolded aggregate.