4y5r | pdb_00004y5r

Crystal Structure of a T67A MauG/pre-Methylamine Dehydrogenase Complex

spinqualitylabelsall models 4y5r, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4y5r is a 6 chain structure with sequence from Paracoccus denitrificans and 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 2.8Å Ligands: 0AF, CA, HEC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MAUG_PARDP Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH. Publication Abstract from PubMed The diheme enzyme MauG catalyzes a six-electron oxidation required for posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. One heme is low-spin with ligands provided by His205 and Tyr294, and the other is high-spin with a ligand provided by His35. The side chain methyl groups of Thr67 and Leu70 are positioned at a distance of 3.4A on either side of His35, maintaining a hydrophobic environment in the proximal pocket of the high-spin heme and restricting the movement of this ligand. Mutation of Thr67 to Ala in the proximal pocket of the high-spin heme prevented reduction of the low-spin heme by dithionite, yielding a mixed-valent state. The mutation also enhanced the stabilization of the charge-resonance-transition of the high-valent bis-Fe(IV) state that is generated by addition of H2O2. The rates of electron transfer from TTQ biosynthetic intermediates to the high-valent form of T67A MauG were similar to that of wild-type MauG. These results are compared to those previously reported for mutation of residues in the distal pocket of the high-spin heme that also affected the redox properties and charge resonance transition stabilization of the high-valent state of the hemes. However, given the position of residue 67, the structure of the variant protein and the physical nature of the T67A mutation, the basis for the effects of the T67A mutation must be different from those of the mutations of the residues in the distal heme pocket. A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent Fe(II)/Fe(III) state and enhances charge resonance stabilization of the bis-Fe(IV) state.,Shin S, Feng M, Li C, Williamson HR, Choi M, Wilmot CM, Davidson VL Biochim Biophys Acta. 2015 Aug;1847(8):709-16. doi: 10.1016/j.bbabio.2015.04.008., Epub 2015 Apr 17. PMID:25896561 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methylamine dehydrogenase Methylamine utilisation protein Methylation utilization protein MauG

Proteopedia Page Contributors and Editors (what is this?)

OCA