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2c2u

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(New page: 200px<br /> <applet load="2c2u" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c2u, resolution 1.10&Aring;" /> '''DPS FROM DEINOCOCCU...)
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Revision as of 14:46, 29 October 2007

Image:2c2u.gif

2c2u, resolution 1.10Å

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DPS FROM DEINOCOCCUS RADIODURANS

Overview

The crystal structure of a DNA-binding protein from starved cells (Dps), (DR2263) from Deinococcus radiodurans was determined in two states: a, native form, to 1.1-A resolution, and one soaked in an iron solution, to, 1.6-A resolution. In comparison with other Dps proteins, DR2263 has an, extended N-terminal extension, in both structures presented here, a novel, metal binding site was identified in this N-terminal extension and was, assigned to bound zinc. The zinc is tetrahedrally coordinated and the, ligands, that belong to the N-terminal extension, are two histidines, one, glutamate and one aspartate residue, which are unique to this protein, within the Dps family. In the iron-soaked crystal structure, a total of, three iron sites per monomer were found: one site corresponds to the, ... [(full description)]

About this Structure

2C2U is a [Single protein] structure of sequence from [Deinococcus radiodurans] with SO4, ZN and FE as [ligands]. Full crystallographic information is available from [OCA].

Reference

The crystal structure of Deinococcus radiodurans Dps protein (DR2263) reveals the presence of a novel metal centre in the N terminus., Romao CV, Mitchell EP, McSweeney S, J Biol Inorg Chem. 2006 Oct;11(7):891-902. Epub 2006 Jul 20. PMID:16855817

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