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1w68

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[[Category: tyrosyl radical]]
[[Category: tyrosyl radical]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:50:22 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:26:18 2007''

Revision as of 14:21, 30 October 2007

Image:1w68.gif

1w68, resolution 2.20Å

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CRYSTAL STRUCTURE OF MOUSE RIBONUCLEOTIDE REDUCTASE SUBUNIT R2 UNDER OXIDIZING CONDITIONS. A FULLY OCCUPIED DINUCLEAR IRON CLUSTER.

Overview

Class I ribonucleotide reductase (RNR) catalyzes the de novo synthesis of, deoxyribonucleotides in mammals and many other organisms. The RNR subunit, R2 contains a dinuclear iron center, which in its diferrous form, spontaneously reacts with O2, forming a mu-oxo-bridged diferric cluster, and a stable tyrosyl radical. Here, we present the first crystal, structures of R2 from mouse with its native dinuclear iron center, both, under reducing and oxidizing conditions. In one structure obtained under, reducing conditions, the iron-bridging ligand Glu-267 adopts the, mu-(eta1,eta2) coordination mode, which has previously been related to O2, activation, and an acetate ion from the soaking solution is observed where, O2 has been proposed to bind the iron. The structure of mouse R2 under, ... [(full description)]

About this Structure

1W68 is a [Single protein] structure of sequence from [Mus musculus] with FEO as [ligand]. Active as [Ribonucleoside-diphosphate reductase], with EC number [1.17.4.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structural studies of changes in the native dinuclear iron center of ribonucleotide reductase protein R2 from mouse., Strand KR, Karlsen S, Kolberg M, Rohr AK, Gorbitz CH, Andersson KK, J Biol Chem. 2004 Nov 5;279(45):46794-801. Epub 2004 Aug 17. PMID:15322079

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