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 Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis. A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis. FEBS Lett. (0014-5793) 2013 Abu Tarboush N., Jensen LM., Wilmot CM., Davidson VL. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Abu Tarboush N., Jensen LM., Wilmot CM., Davidson VL. FEBS Lett. (0014-5793) 2013 a1bba0_pardp Methylamine dehydrogenase (amicyanin) Pden_4733 protein protein pardp Paracoccus denitrificans (strain Pd 1222) MLGNFRFDDMVEKLSRRVAGQTSRRSVIGKLGTAMLGIGLVPLLPVDRRGRVSRANAADAPAGTDPRAKWVPQDNDIQACDYWRHCSIDGNICDCSGGSLTNCPPGTKLATASWVASCYNPTDGQSYLIAYRDCCGYNVSGRCPCLNTEGELPVYRPEFANDIIWCFGAEDDAMTYHCTISPIVGKAS mint E3D9DE4454268BE8 a1bb97_pardp Methylamine dehydrogenase (amicyanin) Methylamine dehydrogenase heavy chain Pden_4730 protein protein pardp Paracoccus denitrificans (strain Pd 1222) MALPPNFMPLFRASLIGLGLGCSALALAASAQDAPEAETQAQETQGQAAARAAAADLAAGQDDEPRILEAPAPDARRVYVNDPAHFAAVTQQFVIDGEAGRVIGMIDGGFLPNPVVADDGSFIAHASTVFSRIARGERTDYVEVFDPVTLLPTADIELPDAPRFLVGTYPWMTSLTPDGKTLLFYQFSPAPAVGVVDLEGKAFKRMLDVPDCYHIFPTAPDTFFMHCRDGSLAKVAFGTEGTPEITHTEVFHPEDEFLINHPAYSQKAGRLVWPTYTGKIHQIDLSSGDAKFLPAVEALTEAERADGWRPGGWQQVAYHRALDRIYLLVDQRDEWRHKTASRFVVVLDAKTGERLAKFEMGHEIDSINVSQDEKPLLYALSTGDKTLYIHDAESGEELRSVNQLGHGPQVITTADMG mint 819B4EEE2AC6D340 maug_pardp Methylamine utilization protein MauG mauG Pden_4736 protein protein pardp Paracoccus denitrificans (strain Pd 1222) MLRLACLAPLAILIPAAGTAEQARPADDALAALGAQLFVDPALSRNATQSCATCHDPARAFTDPREGKAGLAVSVGDDGQSHGDRNTPTLGYAALVPAFHRDANGKYKGGQFWDGRADDLKQQAGQPMLNPVEMAMPDRAAVAARLRDDPAYRTGFEALFGKGVLDDPERAFDAAAEALAAYQATGEFSPFDSKYDRVMRGEEKFTPLEEFGYTVFITWNCRLCHMQRKQGVAERETFTNFEYHNIGLPVNETAREASGLGADHVDHGLLARPGIEDPAQSGRFKVPSLRNVAVTGPYMHNGVFTDLRTAILFYNKYTSRRPEAKINPETGAPWGEPEVARNLSLAELQSGLMLDDGRVDALVAFLETLTDRRYEPLLEESRAAQKD mint DDC9618235D6838E a1bb97-a1bba0 1 MauG 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 1.5 preMADH light chain 2 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.4 preMADH heavy chain 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 3.3 physical association physical association mint PDB code: 3RN1 W199E MauG was co-crystallized with preMADH and the X-ray crystal structure solved to a resolution of 1.93 Å. Data collection and refinement statistics are given in Table 1. The W199E-MauG/preMADH complex (PDB entry 3RN1) has the same overall structure as that of the WT MauG/preMADH complex (PDB entry 3L4M), with two crystallographically independent copies of W199E MauG in the asymmetric unit (RMSD values on Cα positions in the range of 0.15 0.32 Å). The positions of the nascent TTQ sites, both hemes and the intervening Trp93 residue are preserved in W199E MauG. The position of Glu199 at the interface of MauG and preMADH is essentially the same as that of the native Trp199 residue (Fig. 6A). In the WT MauG/preMADH crystal structure, Glu101 of the preMADH β-subunit is the only preMADH residue that directly contacts Trp199, whose indole nitrogen forms a weak hydrogen bond with the side chain of βGlu101 (3.2 Å) (Fig. 6B). t1 f6a f6b