4AU9

Crystal Structure of a Fungal DyP-Type Peroxidase from Auricularia auricula-judae

Summary for 4AU9

• Entry DOI: 10.2210/pdb4au9/pdb
• Descriptor: DYP-TYPE PEROXIDASE I, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: oxidoreductase, heme, glycoprotein
• Biological source: AURICULARIA AURICULA-JUDAE (EAR FUNGUS)
• Total number of polymer chains: 2
• Total formula weight: 97656.50

Authors

Strittmatter, E.,Pecyna, M.,Ullrich, R.,Hofrichter, M.,Plattner, D.A.,Liers, C.,Piontek, K. (deposition date: 2012-05-14, release date: 2012-12-26, Last modification date: 2024-11-13)

Primary citation

Strittmatter, E.,Liers, C.,Ullrich, R.,Wachter, S.,Hofrichter, M.,Plattner, D.A.,Piontek, K.
First Crystal Structure of a Fungal High-Redox Potential Dye-Decolorizing Peroxidase: Substrate Interaction Sites and Long-Range Electron Transfer.
J.Biol.Chem., 288:4095-, 2013

PubMed Abstract: Dye-decolorizing peroxidases (DyPs) belong to the large group of heme peroxidases. They utilize hydrogen peroxide to catalyze oxidations of various organic compounds. AauDyPI from Auricularia auricula-judae (fungi) was crystallized, and its crystal structure was determined at 2.1 Å resolution. The mostly helical structure also shows a β-sheet motif typical for DyPs and Cld (chlorite dismutase)-related structures and includes the complete polypeptide chain. At the distal side of the heme molecule, a flexible aspartate residue (Asp-168) plays a key role in catalysis. It guides incoming hydrogen peroxide toward the heme iron and mediates proton rearrangement in the process of Compound I formation. Afterward, its side chain changes its conformation, now pointing toward the protein backbone. We propose an extended functionality of Asp-168, which acts like a gatekeeper by altering the width of the heme cavity access channel. Chemical modifications of potentially redox-active amino acids show that a tyrosine is involved in substrate interaction. Using spin-trapping experiments, a transient radical on the surface-exposed Tyr-337 was identified as the oxidation site for bulky substrates. A possible long-range electron transfer pathway from the surface of the enzyme to the redox cofactor (heme) is discussed.

PubMed: 23235158
DOI: 10.1074/JBC.M112.400176

Experimental method

X-RAY DIFFRACTION (2.1 Å)