3PXW

Crystal Structure of Ferrous NO Adduct of MauG in Complex with Pre-Methylamine Dehydrogenase

Summary for 3PXW

• Entry DOI: 10.2210/pdb3pxw/pdb
• Related: 3L4M 3L4O 3ORV 3PXS 3PXT 3PXW
• Descriptor: Methylamine utilization protein MauG, TRIETHYLENE GLYCOL, 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE, ... (12 entities in total)
• Functional Keywords: oxidoreductase, electron transport, periplasmic space, 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: 200184.53

Authors

Yukl, E.T.,Goblirsch, B.R.,Wilmot, C.M. (deposition date: 2010-12-10, release date: 2011-03-23, Last modification date: 2024-11-06)

Primary citation

Yukl, E.T.,Goblirsch, B.R.,Davidson, V.L.,Wilmot, C.M.
Crystal Structures of CO and NO Adducts of MauG in Complex with Pre-Methylamine Dehydrogenase: Implications for the Mechanism of Dioxygen Activation.
Biochemistry, 50:2931-2938, 2011

PubMed Abstract: MauG is a diheme enzyme responsible for the post-translational formation of the catalytic tryptophan tryptophylquinone (TTQ) cofactor in methylamine dehydrogenase (MADH). MauG can utilize hydrogen peroxide, or molecular oxygen and reducing equivalents, to complete this reaction via a catalytic bis-Fe(IV) intermediate. Crystal structures of diferrous, Fe(II)-CO, and Fe(II)-NO forms of MauG in complex with its preMADH substrate have been determined and compared to one another as well as to the structure of the resting diferric MauG-preMADH complex. CO and NO each bind exclusively to the 5-coordinate high-spin heme with no change in ligation of the 6-coordinate low-spin heme. These structures reveal likely roles for amino acid residues in the distal pocket of the high-spin heme in oxygen binding and activation. Glu113 is implicated in the protonation of heme-bound diatomic oxygen intermediates in promoting cleavage of the O-O bond. Pro107 is shown to change conformation on the binding of each ligand and may play a steric role in oxygen activation by positioning the distal oxygen near Glu113. Gln103 is in a position to provide a hydrogen bond to the Fe(IV)═O moiety that may account for the unusual stability of this species in MauG.

PubMed: 21355604
DOI: 10.1021/bi200023n

Experimental method

X-RAY DIFFRACTION (2.11 Å)