2zhg

Crystal structure of SoxR in complex with DNA

spinqualitylabelsall models 2zhg, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zhg is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: DTT, FES, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SOXR_ECOLI Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron-sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress. Upon reduction of 2Fe-2S cluster, SoxR reversibly loses its transcriptional activity, but retains its DNA binding affinity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The [2Fe-2S] transcription factor SoxR, a member of the MerR family, functions as a bacterial sensor of oxidative stress such as superoxide and nitric oxide. SoxR is activated by reversible one-electron oxidation of the [2Fe-2S] cluster and then enhances the production of various antioxidant proteins through the soxRS regulon. In the active state, SoxR and other MerR family proteins activate transcription from unique promoters, which have a long 19- or 20-bp spacer between the -35 and -10 operator elements, by untwisting the promoter DNA. Here, we show the crystal structures of SoxR and its complex with the target promoter in the oxidized (active) state. The structures reveal that the [2Fe-2S] cluster of SoxR is completely solvent-exposed and surrounded by an asymmetric environment stabilized by interaction with the other subunit. The asymmetrically charged environment of the [2Fe-2S] cluster probably causes redox-dependent conformational changes of SoxR and the target promoter. Compared with the promoter structures with the 19-bp spacer previously studied, the DNA structure is more sharply bent, by approximately 1 bp, with the two central base pairs holding Watson-Crick base pairs. Comparison of the target promoter sequences of the MerR family indicates that the present DNA structure represents the activated conformation of the target promoter with a 20-bp spacer in the MerR family. Crystal structure of the [2Fe-2S] oxidative-stress sensor SoxR bound to DNA.,Watanabe S, Kita A, Kobayashi K, Miki K Proc Natl Acad Sci U S A. 2008 Mar 18;105(11):4121-6. Epub 2008 Mar 11. PMID:18334645 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transcriptional activator 3D structures

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