2clb

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Revision as of 16:59, 29 October 2007

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spinqualitylabelsall models 2clb, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THE STRUCTURE OF THE DPS-LIKE PROTEIN FROM SULFOLOBUS SOLFATARICUS REVEALS A BACTERIOFERRITIN-LIKE DI-METAL BINDING SITE WITHIN A DPS-LIKE DODECAMERIC ASSEMBLY

Overview

The superfamily of ferritin-like proteins has recently expanded to include, a phylogenetically distinct class of proteins termed DPS-like (DPSL), proteins. Despite their distinct genetic signatures, members of this, subclass share considerable similarity to previously recognized DPS, proteins. Like DPS, these proteins are expressed in response to oxidative, stress, form dodecameric cage-like particles, preferentially utilize, H(2)O(2) in the controlled oxidation of Fe(2+), and possess a short, N-terminal extension implicated in stabilizing cellular DNA. Given these, extensive similarities, the functional properties responsible for the, preservation of the DPSL signature in the genomes of diverse prokaryotes, have been unclear. Here, we describe the crystal structure of a DPSL, protein ... [(full description)]

About this Structure

2CLB is a [Single protein] structure of sequence from [Sulfolobus solfataricus] with ZN and FE as [ligands]. Full crystallographic information is available from [OCA].

Reference

Structure of the DPS-like protein from Sulfolobus solfataricus reveals a bacterioferritin-like dimetal binding site within a DPS-like dodecameric assembly., Gauss GH, Benas P, Wiedenheft B, Young M, Douglas T, Lawrence CM, Biochemistry. 2006 Sep 12;45(36):10815-27. PMID:16953567

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