4FB1

Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 60 Days

4FB1 の概要

• エントリーDOI: 10.2210/pdb4fb1/pdb
• 関連するPDBエントリー: 3L4M 4FA4 4FA5 4FA9 4FAN 4FAV
• 分子名称: Methylamine utilization protein MauG, Methylamine dehydrogenase light chain, Methylamine dehydrogenase heavy chain, ... (8 entities in total)
• 機能のキーワード: trytpophan tryptophylquinone, oxidoreductase-electron transfe complex, oxidoreductase-electron transfer complex, oxidoreductase/electron transfer
• 由来する生物種: Paracoccus denitrificans; 詳細
• 細胞内の位置: Periplasm: Q51658 P22619
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 200000.36

構造登録者

Yukl, E.T.,Wilmot, C.M. (登録日: 2012-05-22, 公開日: 2013-03-27, 最終更新日: 2024-10-30)

主引用文献

Yukl, E.T.,Liu, F.,Krzystek, J.,Shin, S.,Jensen, L.M.,Davidson, V.L.,Wilmot, C.M.,Liu, A.
Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis.
Proc.Natl.Acad.Sci.USA, 110:4569-4573, 2013

PubMed Abstract: Despite the importance of tryptophan (Trp) radicals in biology, very few radicals have been trapped and characterized in a physiologically meaningful context. Here we demonstrate that the diheme enzyme MauG uses Trp radical chemistry to catalyze formation of a Trp-derived tryptophan tryptophylquinone cofactor on its substrate protein, premethylamine dehydrogenase. The unusual six-electron oxidation that results in tryptophan tryptophylquinone formation occurs in three discrete two-electron catalytic steps. Here the exact order of these oxidation steps in the processive six-electron biosynthetic reaction is determined, and reaction intermediates are structurally characterized. The intermediates observed in crystal structures are also verified in solution using mass spectrometry. Furthermore, an unprecedented Trp-derived diradical species on premethylamine dehydrogenase, which is an intermediate in the first two-electron step, is characterized using high-frequency and -field electron paramagnetic resonance spectroscopy and UV-visible absorbance spectroscopy. This work defines a unique mechanism for radical-mediated catalysis of a protein substrate, and has broad implications in the areas of applied biocatalysis and understanding of oxidative protein modification during oxidative stress.

PubMed: 23487750
DOI: 10.1073/pnas.1215011110

実験手法

X-RAY DIFFRACTION (2.15 Å)