Methylamine utilisation protein

spinqualitylabelsall models MauG containing hydroxytryptophan (grey, green) complex with MADH light chain (magenta, pink), MADH heavy chain (yellow, cyan), acetate, PEG, tetra ethylene glycol Na+, Ca+2 (PDB ID 3pxt) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Methylamine utilisation protein. (MauG) is a 2 c type heme protein (in which the heme is covalently bound to the protein) which catalyses the post translational modification of tryptophan cryptophilquinone biosynthesis within methylamine dehydrogenase (MADH). The catalysis process is a remote one involving hole hopping mechanism of electron transfer in which Trp residues are reversibly oxidized. MauG catalyses the 6-electron oxidation of MADH using hydrogen peroxide or oxygen. Structural highlights The type c heme moiety is coordinated to 5 MauG residues. 3D structures of MauG Updated on 09-August-2022 3l4m, 3pxs, 4fa1, 4fa4, 4fa5, 4fa9, 4fan, 4fav, 4fb1 – PdMauG + MADH – Paracoccus dentrificans 3orv, 3sle, 3rlm, 3rmz, 3rn0, 3rn1, 3sjl, 3svw, 4l1q, 4l3g, 4l3h, 4o1q, 4y5r – PdMauG (mutant) + MADH 3sxt, 4k3i – PdMauG + MADH (quinol) 3sws – PdMauG + MADH (quinone) 3pxw – PdMauG + MADH + NO 3pxt – PdMauG + MADH + CO

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