2boq

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spinqualitylabelsall models 2boq, resolution 1.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF VERSATILE PEROXIDASE

Overview

Versatile peroxidases (VP), a recently described family of ligninolytic, peroxidases, show a hybrid molecular architecture combining different, oxidation sites connected to the heme cofactor. High-resolution crystal, structures as well as homology models of VP isoenzymes from the fungus, Pleurotus eryngii revealed three possibilities for long-range electron, transfer for the oxidation of high redox potential aromatic compounds. The, possible pathways would start either at Trp164 or His232 of isoenzyme VPL, and at His82 or Trp170 of isoenzyme VPS1. These residues are exposed, and, less than 11 A apart from the heme. With the purpose of investigating, their functionality, two single mutations (W164S and H232F) and one double, mutation (W164S/P76H) were introduced in VPL that: (i) removed ... [(full description)]

About this Structure

2BOQ is a [Single protein] structure of sequence from [Pleurotus eryngii] with ZN, MN, CAC, CA and HEM as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways., Perez-Boada M, Ruiz-Duenas FJ, Pogni R, Basosi R, Choinowski T, Martinez MJ, Piontek K, Martinez AT, J Mol Biol. 2005 Nov 25;354(2):385-402. Epub 2005 Oct 3. PMID:16246366

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