3L4M

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

Summary for 3L4M

• Entry DOI: 10.2210/pdb3l4m/pdb
• Related: 3L4O 3ORV 3PXS 3PXT 3PXW
• Descriptor: Methylamine utilization protein mauG, Methylamine dehydrogenase light chain, Methylamine dehydrogenase heavy chain, ... (9 entities in total)
• Functional Keywords: maug, methylamine dehydrogenase, quinone cofactor, ttq, his-tyr heme, electron transport, c-heme, iron, metal-binding, oxidoreductase, transport, disulfide bond, oxidoreductase-electron transport complex, oxidoreductase/electron transport
• Biological source: Paracoccus denitrificans; More
• Cellular location: Periplasm: Q51658 P22619
• Total number of polymer chains: 6
• Total formula weight: 200288.72

Authors

Jensen, L.M.R.,Wilmot, C.M. (deposition date: 2009-12-21, release date: 2010-03-23, Last modification date: 2024-11-06)

Primary citation

Jensen, L.M.,Sanishvili, R.,Davidson, V.L.,Wilmot, C.M.
In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex.
Science, 327:1392-1394, 2010

PubMed Abstract: 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 betaTrp57, to fully functional MADH by catalyzing the insertion of a second oxygen atom into the indole ring and covalently linking betaTrp57 to betaTrp108. 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.

PubMed: 20223990
DOI: 10.1126/science.1182492

Experimental method

X-RAY DIFFRACTION (2.02 Å)