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 guettou-2013-3 Structural insights into substrate recognition in proton-dependent oligopeptide transporters. in vitro In vitro crosslink cross-linking study crosslink weight by staining molecular weight estimation by staining weight by staining Guettou F., Quistgaard E.M., Trésaugues L., Moberg P., Jegerschöld C., Zhu L., Jong A.J., Nordlund P., Löw C. par.nordlund@ki.se EMBO Rep. (1469-221X) 2013 Only protein-protein interactions imex curation guettou-2013-4 Structural insights into substrate recognition in proton-dependent oligopeptide transporters. in vitro In vitro bn-page blue native page bn-page weight by staining molecular weight estimation by staining weight by staining Guettou F., Quistgaard E.M., Trésaugues L., Moberg P., Jegerschöld C., Zhu L., Jong A.J., Nordlund P., Löw C. par.nordlund@ki.se EMBO Rep. (1469-221X) 2013 Only protein-protein interactions imex curation guettou-2013-1 Structural insights into substrate recognition in proton-dependent oligopeptide transporters. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Guettou F., Quistgaard E.M., Trésaugues L., Moberg P., Jegerschöld C., Zhu L., Jong A.J., Nordlund P., Löw C. par.nordlund@ki.se EMBO Rep. (1469-221X) 2013 Only protein-protein interactions imex curation guettou-2013-2 Structural insights into substrate recognition in proton-dependent oligopeptide transporters. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Guettou F., Quistgaard E.M., Trésaugues L., Moberg P., Jegerschöld C., Zhu L., Jong A.J., Nordlund P., Löw C. par.nordlund@ki.se EMBO Rep. (1469-221X) 2013 Only protein-protein interactions imex curation guettou-2013-5 Structural insights into substrate recognition in proton-dependent oligopeptide transporters. in vitro In vitro electron microscopy electron microscopy Electron crystallography Electron cryomicroscopy Electron crystallography Electron cryomicroscopy predetermined predetermined participant predetermined Guettou F., Quistgaard E.M., Trésaugues L., Moberg P., Jegerschöld C., Zhu L., Jong A.J., Nordlund P., Löw C. par.nordlund@ki.se EMBO Rep. (1469-221X) 2013 Only protein-protein interactions imex curation q8ehe6_sheon SO_1277 protein protein sheon Shewanella oneidensis (strain MR-1) MTLGTNQVSKTHSFMTVSLIELWERFGYYGMQALIVYFMVQRLGFDDSRANLVWSACAALIYVSPAIGGWVGDKILGTKRTMLLGAGILSVGYALMTVPTENTWFMFSALGVIVVGNGLFKPNAGNLVRKIYEGDDSKIDSAFTIYYMAVNVGSTFSMLLTPWIKDYVNAQYGNEFGWHAAFAVCCVGILVGLGNYALMHKSLANYGSEPDTRPVNKKSLAIVLALAALSVVASAIILEYEDVARVFVYAAGVAVLGIFFHLIRTSEPSERAGLIAALILTVQTVFFFIFYQQMSTSLALFALRNVDWDFQVFGTHLWTWSPAQFQALNPIWIMVLSPVLAWSYSWAGRNNKDFSIAAKFALGFAVVAIGFFIYGFAGQFAVNGKTSSWVMIWGYASYSLGELLVSGLGLAMIARYVPARMGGFMMGAYFVASGISQYLGGVVANFASVPQDLVDPLQTLPVYTNLFNKLGVAAVVCTIIALAVLPLMRRLTESHHAHSSIENNAAASLRDVKAEQ q5m4h8_strt2 dtpT stu0970 protein protein strt2 Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) MEDKGKTFFGQPLGLSTLFMTEMWERFSYYGMRAILLYYMWFLISTGDLHITRATAASIMAIYASMVYLSGTIGGFVADRIIGARPAVFWGGVLIMLGHIVLALPFGASALFGSIILIIIGTGFLKPNVSTLVGTLYDEHDRRRDAGFSIFVFGINLGAFIAPLIVGAAQEAAGYHVAFSLAAIGMFIGLLVYYFGGKKTLDPHYLRPTDPLAPEEVKPLLVKVSLAVAGFIAIIVVMNLVGWNSLPAYINLLTIVAIAIPVFYFAWMISSVKVTSTEHLRVVSYIPLFIAAVLFWAIEEQGSVVLATFAAERVDSSWFPVSWFQSLNPLFIMLYTPFFAWLWTAWKKNQPSSPTKFAVGLMFAGLSFLLMAIPGALYGTSGKVSPLWLVGSWALVILGEMLISPVGLSVTTKLAPKAFNSQMMSMWFLSSSVGSALNAQLVTLYNAKSEVAYFSYFGLGSVVLGIVLVFLSKRIQGLMQGVE q8ehe6-1 1459453 n/a 1459458 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false f4b q8ehe6-1 1459453 n/a 1459458 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 3.0 direct interaction direct interaction false false false f4b q8ehe6-1 1459453 n/a 1459458 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false f4b dtpt 1459453 n/a 1459459 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false f4b q8ehe6-1 1459454 n/a 1459458 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false f4c dtpt-1 1459454 n/a 1459459 weight by staining molecular weight estimation by staining weight by staining unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false f4c q8ehe6 1459455 n/a 1459458 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false f1a f2a f2b f2c st1 sf6 sf7 The crystal form used for the structure determination of PepTSo2 is in a dimeric conformation. This dimer interface appears to be stabilized by the presence of a zinc ion and is most likely a crystal-packing artefact (supplementary Figs 6 and 7 online). However, a second crystal form of PepTSo2 in spacegroup P3121, diffracting to 4.6A° resolution, was obtained in a crystallization condition in the absence of zinc, and molecular replacement into this form did indeed show a tetrameric assembly in the crystal lattice, which might correspond to the tetramer visible in the EM experiments (Fig 4E). Both structures mainly differ in the position of TM12, which mediates key interactions in the oligomeric assembly (Fig 4E,F). Higher resolution data of this crystal form and more functional data will be necessary to unravel potential structural differences of transporter units within the tetramer and the relevance of the oligomerization q8ehe6-q8ehe6 1459456 n/a 1459458 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified n/a 1459458 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false f4a While screening various POTs for structural studies, we realized that PepTSo2 elutes after significantly shorter retention times on an analytical gel filtration column compared to previously characterized POTs (Fig 4A), indicative of a higher oligomer assembly. q8ehe6-1 1459457 n/a 1459458 unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false f4d f4e f4f