1qo4

From Proteopedia

Revision as of 13:57, 30 October 2007

ARABIDOPSIS THALIANA PEROXIDASE A2 AT ROOM TEMPERATURE

Overview

Anionic Arabidopsis thaliana peroxidase ATP A2 was expressed in, Escherichia coli and used as a model for the 95% identical commercially, available horseradish peroxidase HRP A2. The crystal structure of ATP A2, at 1.45 A resolution at 100 K showed a water molecule only 2.1 A from heme, iron [Ostergaard, L., et al. (2000) Plant Mol. Biol. 44, 231-243], whereas, spectroscopic studies of HRP A2 in solution at room temperature [Feis, A., et al. (1998) J. Raman Spectrosc. 29, 933-938] showed five-coordinated, heme iron, which is common in peroxidases. Presented here, the X-ray, crystallographic, single-crystal, and solution resonance Raman studies at, room temperature confirmed that the sixth coordination position of heme, iron of ATP A2 is essentially vacant. Furthermore, electronic ... [(full description)]

About this Structure

1QO4 is a [Single protein] structure of sequence from [Arabidopsis thaliana] with CA and HEM as [ligands]. Active as [Peroxidase], with EC number [1.11.1.7]. Structure known Active Sites: CA1, CA2 and HEM. Full crystallographic information is available from [OCA].

Reference

Differential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2., Nielsen KL, Indiani C, Henriksen A, Feis A, Becucci M, Gajhede M, Smulevich G, Welinder KG, Biochemistry. 2001 Sep 18;40(37):11013-21. PMID:11551197

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