5vj0

Crystal Structure of heme-containing DyP Type Peroxidase from Enterobacter lignolyticus

spinqualitylabelsall models 5vj0, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vj0 is a 4 chain structure with sequence from "enterobacter_lignolyticus"_deangelis_et_al._2011 "enterobacter lignolyticus" deangelis et al. 2011. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM Gene: YfeX ("Enterobacter lignolyticus" Deangelis et al. 2011) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Dye-decolorizing peroxidases (DyPs) are a family of H2O2-dependent heme peroxidases, which have shown potential applications in lignin degradation and valorization. However, the DyP kinetic mechanism remains underexplored. Using structural biology and solvent isotope (sKIE) and viscosity effects, many mechanistic characteristics have been uncovered for the B-class ElDyP from Enterobacter lignolyticus. Its structure revealed that a water molecule acts as the sixth axial ligand with two channels at diameters of ~3.0 and 8.0 A leading to the heme center. A conformational change of ERS(*) to ERS, which have identical spectral characteristics, was proposed as the final step in DyPs' bisubstrate Ping-Pong mechanism. This step is also the rate-determining step in ABTS oxidation. The normal KIE of wild-type ElDyP with D2O2 at pH 3.5 suggested that cmpd 0 deprotonation by the distal aspartate is rate-limiting in the formation of cmpd I, which is more reactive under acidic pH than under neutral or alkaline pH. The viscosity effects and other biochemical methods implied that the reducing substrate binds with cmpd I instead of the free enzyme. The significant inverse sKIEs of kcat/KM and kERS* suggested that the aquo release in DyPs is mechanistically important and may explain the enzyme's adoption of two-electron reduction for cmpd I. The distal aspartate is catalytically more important than the distal arginine and plays key roles in determining DyPs' acidic pH optimum. The kinetic mechanism of D143H-ElDyP was also briefly studied. The results obtained will pave the way for future protein engineering to improve DyPs' lignolytic activity. Mechanistic Insights into Dye-Decolorizing Peroxidase Revealed by Solvent Isotope and Viscosity Effects.,Shrestha R, Huang G, Meekins DA, Geisbrecht BV, Li P ACS Catal. 2017 Sep 1;7(9):6352-6364. doi: 10.1021/acscatal.7b01861. Epub 2017, Aug 9. PMID:29308295 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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