4fa1

Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 130 Days.Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 130 Days.

Structural highlights 4fa1 is a 6 chain structure with sequence from Atcc 17741 and Pardp. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , , , NonStd Res: Related: 3l4m, 4fa4, 4fa5, 4fa9, 4fan, 4fb1 Gene: mauG, Pden_4736 (PARDP), mauA (ATCC 17741), Pden_4730 (PARDP) Activity: Methylamine dehydrogenase (amicyanin), with EC number 1.4.9.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MAUG_PARDP] Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH. [DHML_PARDE] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. Publication Abstract from PubMed 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. Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis.,Yukl ET, Liu F, Krzystek J, Shin S, Jensen LM, Davidson VL, Wilmot CM, Liu A Proc Natl Acad Sci U S A. 2013 Mar 19;110(12):4569-73. doi:, 10.1073/pnas.1215011110. Epub 2013 Mar 4. PMID:23487750 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methylamine dehydrogenase Methylation utilization protein MauG

spinqualitylabelsall models 4fa1, resolution 2.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image