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

Nafez Abu Tarboush, Lyndal M.R. Jensen, Carrie M. Wilmot, Victor L. Davidson

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1736-1741
Number of pages6
JournalFEBS Letters
Volume587
Issue number12
DOIs
StatePublished - Jun 19 2013

Bibliographical note

Funding Information:
We thank Dr. Aimin Liu and Jiafeng Geng at Georgia State University for performing the EPR experiments and providing Fig. 4 , and Yu Tang for technical assistance. This work was supported by NIH Grants GM41574 (VLD) and GM66569 (CMW) and a Minnesota Partnership for Biotechnology and Medical Genomics Grant SPAP-05-0013-P-FY06 (CMW). Computer resources were provided by the Basic Sciences Computing Laboratory of the University of Minnesota Supercomputing Institute. X-ray data were collected at Sector 23, GM/CA-CAT at the Advanced Photon Source (APS), Argonne National Laboratory, Argonne, IL. GM/CA CAT has been funded in whole or in part with Federal funds from the National Cancer Institute (Y1-CO-1020) and the National Institute of General Medical Science (Y1-GM-1104). Use of the APS was supported by the U.S. Department of Energy, Basic Energy Sciences, Office of Science, under contract No. DE-AC02-06CH11357. We thank Ed Hoeffner for Kahlert Structural Biology Laboratory support at The University of Minnesota.

Keywords

  • Cofactor biosynthesis
  • Electron transfer
  • Kinetic mechanism
  • Protein-protein interaction

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