2YP1: Crystallization Of A 45 Kda Peroxygenase- Peroxidase From The Mushroom Agrocybe Aegerita And Structure Determination By Sad Utilizing Only The Haem Iron

Citation:
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.
PDB ID: 2YP1Download
MMDB ID: 114423
PDB Deposition Date: 2012/10/29
Updated in MMDB: 2013/12
Experimental Method:
x-ray diffraction
Resolution: 2.31  Å
Source Organism:
Similar Structures:
Biological Unit for 2YP1: dimeric; determined by author and by software (PISA)
Molecular Components in 2YP1
Label Count Molecule
Proteins (2 molecules)
2
Aromatic Peroxygenase
Molecule annotation
Chemicals (36 molecules)
1
2
2
2
3
17
4
2
5
2
6
3
7
8
* Click molecule labels to explore molecular sequence information.

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