Methylation utilization protein MauG

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== Function ==
== Function ==
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'''Methylation utilisation protein MauG''' or '''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<ref>PMID:24144526</ref>. MauG catalyses the 6-electron oxidation of MADH using hydrogen peroxide or oxygen.
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'''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<ref>PMID:24144526</ref>. MauG catalyses the 6-electron oxidation of MADH using hydrogen peroxide or oxygen.
== Structural highlights ==
== Structural highlights ==
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The type c heme moiety is coordinated to 5 MauG residues<ref>PMID:21355604</ref>.
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<scene name='72/728235/Cv/4'>The type c heme moiety bound to MauG</scene><ref>PMID:21355604</ref>. The <scene name='72/728235/Cv/5'>heme is covalently bound</scene> to the protein.
</StructureSection>
</StructureSection>

Current revision

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 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

References

  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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Michal Harel, Alexander Berchansky, Joel L. Sussman

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