A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis
Abbreviated Journal Title
Electron transfer; Protein-protein interaction; Kinetic mechanism; Cofactor biosynthesis; DIFFERENT FORMS; HEME; INTERMEDIATE; BIOGENESIS; COMPLEX; Biochemistry & Molecular Biology; Biophysics; Cell Biology
MauG catalyzes posttranslational modifications of a methylamine dehydrogenase precursor (preMADH) to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. Trp199 is present at the site of interaction between MauG and preMADH and is critical to this process as it mediates hole hopping during the inter-protein electron transfer that is required for catalysis. Trp199 was converted to Glu and the structure and reactivity of the W199E/preMADH complex were characterized. The results reveal that the nature of residue 199 is also important for productive complex formation between preMADH and MauG. Structured summary of protein interactions: preMADH light chain, preMADH heavy chain and MauG physically interact by X-ray crystallography (View interaction). (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
"A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis" (2013). Faculty Bibliography 2010s. 3586.