In crystallo posttranslational modification within a MauG/Pre-methylamine dehydrogenase complex

Lyndal M.R. Jensen, Ruslan Sanishvili, Victor L. Davidson, Carrie M. Wilmot

Research output: Contribution to journalArticlepeer-review

96 Scopus citations


MauG is a diheme enzyme responsible for the posttranslational modification of two tryptophan residues to form the tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrogenase (MADH MauG converts preMADH, containing monohydroxylated βTrp57, to fully functional MADH by catalyzing the insertion of a second oxygen atom into the indole ring and covalently linking βTrp57 to βTrp108. We have solved the x-ray crystal structure of MauG complexed with preMADH to 2.1 angstroms. The c-type heme irons and the nascent TTQ site are separated by long distances over which electron transfer must occur to achieve catalysis. In addition, one of the hemes has an atypical His-Tyr axial ligation. The crystalline protein complex is catalytically competent; upon addition of hydrogen peroxide, MauG-dependent TTQ synthesis occurs.

Original languageEnglish (US)
Pages (from-to)1392-1394
Number of pages3
Issue number5971
StatePublished - Mar 12 2010


Dive into the research topics of 'In crystallo posttranslational modification within a MauG/Pre-methylamine dehydrogenase complex'. Together they form a unique fingerprint.

Cite this