2YP1
Crystallization of a 45 kDa peroxygenase- peroxidase from the mushroom Agrocybe aegerita and structure determination by SAD utilizing only the haem iron
Summary for 2YP1
| Entry DOI | 10.2210/pdb2yp1/pdb |
| Related | 2YOR |
| Descriptor | AROMATIC PEROXYGENASE, SULFATE ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (12 entities in total) |
| Functional Keywords | oxidoreductase, peroxidase/peroxygenase, unspecific/aromatic peroxygenase, heme, glycoprotein |
| Biological source | AGROCYBE AEGERITA |
| Total number of polymer chains | 4 |
| Total formula weight | 158444.66 |
| Authors | Piontek, K.,Strittmatter, E.,Ullrich, R.,Plattner, D.A.,Hofrichter, M. (deposition date: 2012-10-29, release date: 2013-10-23, Last modification date: 2024-10-23) |
| Primary citation | Piontek, K.,Strittmatter, E.,Ullrich, R.,Grobe, G.,Pecyna, M.J.,Kluge, M.,Scheibner, K.,Hofrichter, M.,Plattner, D.A. Structural Basis of Substrate Conversion in a New Aromatic Peroxygenase: P450 Functionality with Benefits J.Biol.Chem., 288:34767-, 2013 Cited by PubMed Abstract: Aromatic peroxygenases (APOs) represent a unique oxidoreductase sub-subclass of heme proteins with peroxygenase and peroxidase activity and were thus recently assigned a distinct EC classification (EC 1.11.2.1). They catalyze, inter alia, oxyfunctionalization reactions of aromatic and aliphatic hydrocarbons with remarkable regio- and stereoselectivities. When compared with cytochrome P450, APOs appear to be the choice enzymes for oxyfunctionalizations in organic synthesis due to their independence from a cellular environment and their greater chemical versatility. Here, the first two crystal structures of a heavily glycosylated fungal aromatic peroxygenase (AaeAPO) are described. They reveal different pH-dependent ligand binding modes. We model the fitting of various substrates in AaeAPO, illustrating the way the enzyme oxygenates polycyclic aromatic hydrocarbons. Spatial restrictions by a phenylalanine pentad in the active-site environment govern substrate specificity in AaeAPO. PubMed: 24126915DOI: 10.1074/JBC.M113.514521 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.31 Å) |
Structure validation
Download full validation report
