3DTK
Crystal structure of the IRRE protein, a central regulator of DNA damage repair in deinococcaceae
Summary for 3DTK
| Entry DOI | 10.2210/pdb3dtk/pdb |
| Related | 3DTE 3DTI |
| Descriptor | IRRE PROTEIN, CHLORIDE ION, ZINC ION (3 entities in total) |
| Functional Keywords | irre, deinococcus, radiotolerance, gene regulation, metallopeptidase |
| Biological source | deinococcus deserti |
| Total number of polymer chains | 1 |
| Total formula weight | 32503.42 |
| Authors | Vujicic-Zagar, A.,Dulermo, R.,Le Gorrec, M.,Vannier, F.,Servant, P.,Sommer, S.,de Groot, A.,Serre, L. (deposition date: 2008-07-15, release date: 2009-02-17, Last modification date: 2023-11-01) |
| Primary citation | Vujicic-Zagar, A.,Dulermo, R.,Le Gorrec, M.,Vannier, F.,Servant, P.,Sommer, S.,de Groot, A.,Serre, L. Crystal structure of the IrrE protein, a central regulator of DNA damage repair in deinococcaceae J.Mol.Biol., 386:704-716, 2009 Cited by PubMed Abstract: Deinococcaceae are famous for their extreme radioresistance. Transcriptome analysis in Deinococcus radiodurans revealed a group of genes up-regulated in response to desiccation and ionizing radiation. IrrE, a novel protein initially found in D. radiodurans, was shown to be a positive regulator of some of these genes. Deinococcus deserti irrE is able to restore radioresistance in a D. radiodurans DeltairrE mutant. The D. deserti IrrE crystal structure reveals a unique combination of three domains: one zinc peptidase-like domain, one helix-turn-helix motif and one GAF-like domain. Mutant analysis indicates that the first and third domains are critical regions for radiotolerance. In particular, mutants affected in the putative zinc-binding site are as sensitive to gamma and UV irradiation as the DeltairrE bacteria, and radioresistance is strongly decreased with the H217L mutation present in the C-terminal domain. In addition, modeling of IrrE-DNA interaction suggests that the observed IrrE structure may not bind double-stranded DNA through its central helix-turn-helix motif and that IrrE is not a classic transcriptional factor that activates gene expression by its direct binding to DNA. We propose that the putative protease activity of IrrE could be a key element of transcription enhancement and that a more classic transcription factor, possibly an IrrE substrate, would link IrrE to transcription of genes specifically involved in radioresistance. PubMed: 19150362DOI: 10.1016/j.jmb.2008.12.062 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.24 Å) |
Structure validation
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