Methylation utilization protein MauG

Function

Methylation utilization protein MauG or Methylamine utilization 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^[1]. MauG catalyses the 6-electron oxidation of MADH using hydrogen peroxide or oxygen.

Structural highlights

^[2]. The to the protein.

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)

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3D structures of methylation utilization protein MauG3D structures of methylation utilization protein MauG

Updated on 07-September-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

ReferencesReferences

↑ Shin S, Davidson VL. MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis. Arch Biochem Biophys. 2014 Feb 15;544:112-8. doi: 10.1016/j.abb.2013.10.004. Epub, 2013 Oct 19. PMID:24144526 doi:http://dx.doi.org/10.1016/j.abb.2013.10.004
↑ Yukl ET, Goblirsch BR, Davidson VL, Wilmot CM. Crystal Structures of CO and NO Adducts of MauG in Complex with Pre-Methylamine Dehydrogenase: Implications for the Mechanism of Dioxygen Activation. Biochemistry. 2011 Mar 16. PMID:21355604 doi:10.1021/bi200023n

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky

[1] Shin S, Davidson VL. MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis. Arch Biochem Biophys. 2014 Feb 15;544:112-8. doi: 10.1016/j.abb.2013.10.004. Epub, 2013 Oct 19. PMID:24144526 doi:http://dx.doi.org/10.1016/j.abb.2013.10.004

[2] Yukl ET, Goblirsch BR, Davidson VL, Wilmot CM. Crystal Structures of CO and NO Adducts of MauG in Complex with Pre-Methylamine Dehydrogenase: Implications for the Mechanism of Dioxygen Activation. Biochemistry. 2011 Mar 16. PMID:21355604 doi:10.1021/bi200023n

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