Methylation utilization protein MauG
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | <scene name='72/728235/Cv/ | + | <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
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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
- ↑ 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
