3rn0

Crystal Structure of the W199K-MauG/pre-Methylamine Dehydrogenase Complex

spinqualitylabelsall models 3rn0, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rn0 is a 6 chain structure with sequence from Paracoccus denitrificans PD1222. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.91Å Ligands: 0AF, CA, HEC, MES, NA, P6G, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A1BB97_PARDP Publication Abstract from PubMed The diheme enzyme MauG catalyzes the posttranslational modification of the precursor protein of methylamine dehydrogenase (preMADH) to complete biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. Catalysis proceeds through a high valent bis-Fe(IV) redox state and requires long-range electron transfer (ET), as the distance between the modified residues of preMADH and the nearest heme iron of MauG is 19.4 A. Trp199 of MauG resides at the MauG-preMADH interface, positioned midway between the residues that are modified and the nearest heme. W199F and W199K mutations did not affect the spectroscopic and redox properties of MauG, or its ability to stabilize the bis-Fe(IV) state. Crystal structures of complexes of W199F/K MauG with preMADH showed no significant perturbation of the MauG-preMADH structure or protein interface. However, neither MauG variant was able to synthesize TTQ from preMADH. In contrast, an ET reaction from diferrous MauG to quinone MADH, which does not require the bis-Fe(IV) intermediate, was minimally affected by the W199F/K mutations. W199F/K MauGs were able to oxidize quinol MADH to form TTQ, the putative final two-electron oxidation of the biosynthetic process, but with k(cat)/K(m) values approximately 10% that of wild-type MauG. The differential effects of the W199F/K mutations on these three different reactions are explained by a critical role for Trp199 in mediating multistep hopping from preMADH to bis-Fe(IV) MauG during the long-range ET that is required for TTQ biosynthesis. Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis.,Tarboush NA, Jensen LM, Yukl ET, Geng J, Liu A, Wilmot CM, Davidson VL Proc Natl Acad Sci U S A. 2011 Oct 11;108(41):16956-61. Epub 2011 Oct 3. PMID:21969534 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methylamine dehydrogenase Methylamine utilisation protein Methylation utilization protein MauG

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