3DTI
Crystal structure of the IRRE protein, a central regulator of DNA damage repair in deinococcaceae
3DTI の概要
エントリーDOI | 10.2210/pdb3dti/pdb |
関連するPDBエントリー | 3DTE 3DTK |
分子名称 | IRRE protein, ZINC ION (2 entities in total) |
機能のキーワード | irre, deinococcus, radiotolerance, gene regulation, metallopeptidase |
由来する生物種 | deinococcus deserti |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 32402.56 |
構造登録者 | Vujicic-Zagar, A.,Dulermo, R.,Le Gorrec, M.,Vannier, F.,Servant, P.,Sommer, S.,De Groot, A.,Serre, L. (登録日: 2008-07-15, 公開日: 2009-02-10, 最終更新日: 2023-11-01) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.5 Å) |
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