A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis

    Authors

    N. Abu Tarboush; L. M. R. Jensen; C. M. Wilmot;V. L. Davidson

    Comments

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    Abbreviated Journal Title

    FEBS Lett.

    Keywords

    Electron transfer; Protein-protein interaction; Kinetic mechanism; Cofactor biosynthesis; DIFFERENT FORMS; HEME; INTERMEDIATE; BIOGENESIS; COMPLEX; Biochemistry & Molecular Biology; Biophysics; Cell Biology

    Abstract

    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.

    Journal Title

    Febs Letters

    Volume

    587

    Issue/Number

    12

    Publication Date

    1-1-2013

    Document Type

    Article

    Language

    English

    First Page

    1736

    Last Page

    1741

    WOS Identifier

    WOS:000320427400007

    ISSN

    0014-5793

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