3ERE
Crystal structure of the arginine repressor protein from Mycobacterium tuberculosis in complex with the DNA operator
3ERE の概要
| エントリーDOI | 10.2210/pdb3ere/pdb |
| 関連するPDBエントリー | 2ZFZ 3BUE 3CAG |
| 分子名称 | Arginine repressor, 5'-D(*DTP*DTP*DGP*DCP*DAP*DTP*DAP*DAP*DCP*DGP*DAP*DTP*DGP*DCP*DAP*DA)-3', 5'-D(*DTP*DTP*DGP*DCP*DAP*DTP*DCP*DGP*DTP*DTP*DAP*DTP*DGP*DCP*DAP*DA)-3', ... (5 entities in total) |
| 機能のキーワード | mycobacterium tuberculosis, arginine repressor protein, dna binding, argr-operator complex, structural genomics, tb structural genomics, tb structural genomics consortium, tbsgc, amino-acid biosynthesis, arginine biosynthesis, dna-binding, transcription, transcription regulation, dna binding protein-dna complex, dna binding protein/dna |
| 由来する生物種 | Mycobacterium tuberculosis 詳細 |
| 細胞内の位置 | Cytoplasm (Probable): P0A4Y8 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 27449.23 |
| 構造登録者 | Cherney, L.T.,Cherney, M.M.,Garen, C.R.,Lu, G.J.,James, M.N.,TB Structural Genomics Consortium (TBSGC) (登録日: 2008-10-01, 公開日: 2008-10-14, 最終更新日: 2023-09-06) |
| 主引用文献 | Cherney, L.T.,Cherney, M.M.,Garen, C.R.,Lu, G.J.,James, M.N. Crystal structure of the arginine repressor protein in complex with the DNA operator from Mycobacterium tuberculosis. J.Mol.Biol., 384:1330-1340, 2008 Cited by PubMed Abstract: The arginine repressor (ArgR) from Mycobacterium tuberculosis (Mtb) is a gene product encoded by the open reading frame Rv1657. It regulates the L-arginine concentration in cells by interacting with ARG boxes in the promoter regions of the arginine biosynthesis and catabolism operons. Here we present a 2.5-A structure of MtbArgR in complex with a 16-bp DNA operator in the absence of arginine. A biological trimer of the protein-DNA complex is formed via the crystallographic 3-fold symmetry axis. The N-terminal domain of MtbArgR has a winged helix-turn-helix motif that binds to the major groove of the DNA. This structure shows that, in the absence of arginine, the ArgR trimer can bind three ARG box half-sites. It also reveals the structure of the whole MtbArgR molecule itself containing both N-terminal and C-terminal domains. PubMed: 18952097DOI: 10.1016/j.jmb.2008.10.015 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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