Methylation utilization protein MauG

From Proteopedia

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spinqualitylabelsall models MauG (grey, green) complex with preMADH heavy chains (yellow, cyan) light chains (pink, magenta) and heme, triethylene glycol, acetate Ca+2 and Na+ ions (PDB code 4fa1) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function The posttranslational modification of two tryptophan residues in pre-methylamine hydrogenase (preMMADH) to form the tryptophan tryptophylquinone redox cofactor of MADH is catalyzed by methylation utilization protein MauG or methylamine utilization protein MauG[1]. MauG contains 2 c-type heme groups in which the heme is covalently bound to the MauG.

3D structures of methylation utilization protein MauG

Updated on 09-August-2022

3sxt, 4k3i, 3pxs, 4fa1, 4fa4, 4fa5, 4fa9, 4fan, 4fav, 4fb1 - PdMauG + PreMADH α + β - Paracoccus denitrificans
3sjl, 3orv - PdMauG (mutant) + PreMADH α + β (mutant)
4y5r, 3rn1, 3sle, 3svw, 3sws, 4o1q, 3rlm, 3rmz, 3rn0, 4l1q, 4l3g, 4l3h - PdMauG (mutant) + PreMADH α + β
3l4m, 3l4o - PdMauG + PreMADH α + β (mutant)
3pxt - PdMauG + PreMADH α + β + CO
3pxw - PdMauG + PreMADH α + β + NO

References

1. ↑ Wang Y, Graichen ME, Liu A, Pearson AR, Wilmot CM, Davidson VL. MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis. Biochemistry. 2003 Jun 24;42(24):7318-25. PMID:12809487 doi:http://dx.doi.org/10.1021/bi034243q