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 A kinetic model linking protein conformational motions, interflavin electron transfer and electron flux through a dual-flavin enzyme-simulating the reductase activity of the endothelial and neuronal nitric oxide synthase flavoprotein domains. A kinetic model linking protein conformational motions, interflavin electron transfer and electron flux through a dual-flavin enzyme-simulating the reductase activity of the endothelial and neuronal nitric oxide synthase flavoprotein domains. FEBS J. (1742-464X) 2011 Haque MM., Kenney C., Tejero J., Stuehr DJ. in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Haque MM., Kenney C., Tejero J., Stuehr DJ. FEBS J. (1742-464X) 2011 sytm2_arath Threonine--tRNA ligase, chloroplastic/mitochondrial 2 F28I8 At2g04842 EMB2761 Protein EMBRYO DEFECTIVE 2761 Threonyl-tRNA synthetase protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MASSHSLLFSSSFLSKPSSFTSSLRRFVYLPTRQFWPRQRHGFSTVFAVATEPAISSSGPKKAEPSTVVLPSNESSDKLLKIRHTCAHVMAMAVQKLFPDAKVTIGPWIDNGFYYDFDMEPLTDKDLKRIKKEMDRIISRNLPLLREEVSREEAKKRIMAINEPYKMEILDGIKEEPITVYHIGNEWWDLCAGPHVETTGKINKKAVELESVAGAYWRGDEKRQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRIGQDLDLFSIQDEAGGGLVFWHPKGAIVRNIIEESWKKMHVEHGYDLIYTPHVAKADLWKISGHLDFYRENMYDQMEIEDELYQLRPMNCPYHILLYQRKRQSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRGVLDLTEEILSRFGFNKYEVNLSTRPEKSVGGDDIWEKATCALRDALDDKGWSYEVDEGGGAFYGPKIDLKIEDALGRKWQCSTIQVDFNLPQRFDITYVDTNSDKKRPIMIHRAVLGSLERFFGVLIEHYAGDFPLWLSPVQVRVLPVTDNQLEFCKEVSKKLRACGVRAELCHGERLPKLIRNAETQKIPLMAVVGPKEVETGTVTVRSRFGGELGTIPVDDLINKINIAVETRTAL mint 66EA72022DD35AFE to204_arath Mitochondrial import receptor subunit TOM20-4 TOM20-4 Translocase of outer membrane 20 kDa subunit 4 MMG1.2 At5g40930 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MDMQNENERLMVFEHARKVAEATYVKNPLDAENLTRWAGALLELSQFQTEPKQMILEAILKLGEALVIDPKKHDALWLIGNAHLSFGFLSSDQTEASDNFEKASQFFQLAVEEQPESELYRKSLTLASKAPELHTGGTAGPSSNSAKTMKQKKTSEFKYDVFGWVILASYVVAWISFANSQTPVSRQ 156DF3D231EA286C emb2761-tom20_4 1 ThrRS-dTP 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Tom20-4 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified gst tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction mint f5 f6 In summary, we have for the first time characterized the interaction between a dual targeting peptide and the mitochondrial import receptor Tom20. The dTP from AtThrRS was investigated by solution NMR, and we found that the peptide is mainly unstructured, but with tendencies to form an amphipathic α-helical structure in the Nterminal part of the sequence and very weak structural tendencies in the C-terminal half of the sequence, a trait characteristic for intrinsically disordered proteins (IDPs) [31,32,49]. The dual targeting peptide does not appear to bind rigidly to Tom20, but is in a dynamic equilibrium, leading to line-broadening effects in NMR spectra. The two regions identified as having structural propensities are the ones mainly responsible for the binding. This implies that the interaction with Tom20 may share features with the mTP Tom20 interaction, but that also other parts of the targeting sequence take part in the interaction.