1qpa

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Revision as of 14:57, 29 October 2007

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spinqualitylabelsall models 1qpa, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

LIGNIN PEROXIDASE ISOZYME LIP4.65 (PI 4.65)

Overview

The crystal structure of lignin peroxidase (LiP) from the white rot fungus, Phanerochaete chrysosporium was refined to an R-factor of 16.2 % utilizing, synchrotron data in the resolution range from 10 to 1.7 A. The final model, comprises all 343 amino acid residues, 370 water molecules, the heme, four, carbohydrates, and two calcium ions. Lignin peroxidase shows the typical, peroxidase fold and the heme has a close environment as found in other, peroxidases. During refinement of the LiP model an unprecedented, modification of an amino acid was recognized. The surface residue, tryptophan 171 in LiP is stereospecifically hydroxylated at the Cbeta atom, due to an autocatalytic process. We propose that during the catalytic, cycle of LiP a transient radical at Trp171 occurs that is different ... [(full description)]

About this Structure

1QPA is a [Single protein] structure of sequence from [[1]] with NAG, MAN, CA and HEM as [ligands]. Full crystallographic information is available from [OCA].

Reference

The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle., Choinowski T, Blodig W, Winterhalter KH, Piontek K, J Mol Biol. 1999 Feb 26;286(3):809-27. PMID:10024453

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