Crystal Structure of the W199E-MauG/pre-Methylamine Dehydrogenase Complex

Mutagenesis of tryptophan199 reveals that electron hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis

THERE IS A CHIRALITY ERROR AT CA ATOM OF 0AF C 57.

Biomorph mirrors (Kirkpatrick-Baez Configuration)

Drops contained 1uL protein with 3uL reservoir solution. Protein solution: 100uM W199E-MauG and 50uM preMADH in 10mM potassium phosphate pH, 7.5. Reservoir solution contained: 23% w/v PEG 8000, 0.1M sodium acetate, 0.1M MES pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Structure of the WT-MauG/pre-Methylamine Dehydrogenase Complex

Crystal Structure of the WT-MauG/pre-Methylamine Dehydrogenase Complex After Treatment with Hydrogen Peroxide

Crystal Structure of the Y294H-MauG/pre-Methylamine Dehydrogenase Complex

Methylamine utilization protein MauG (E.C.1.-.-.-), Methylamine dehydrogenase light chain (E.C.1.4.99.3), Methylamine dehydrogenase heavy chain (E.C.1.4.99.3)

MauG, methylamine dehydrogenase, c-heme, quinone cofactor, ELECTRON TRANSPORT, Oxidoreductase-electron transport complex