1DCM
STRUCTURE OF UNPHOSPHORYLATED FIXJ-N WITH AN ATYPICAL CONFORMER (MONOMER A)
1DCM の概要
| エントリーDOI | 10.2210/pdb1dcm/pdb |
| 関連するPDBエントリー | 1D5W 1DBW 1DCK |
| 分子名称 | TRANSCRIPTIONAL REGULATORY PROTEIN FIXJ, MAGNESIUM ION (3 entities in total) |
| 機能のキーワード | doubly wound five-stranded beta/alpha fold, nitrogen fixation regulation, transcription |
| 由来する生物種 | Sinorhizobium meliloti |
| 細胞内の位置 | Cytoplasm : P10958 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 27784.32 |
| 構造登録者 | Gouet, P.,Fabry, B.,Guillet, V.,Birck, C.,Mourey, L.,Kahn, D.,Samama, J.P. (登録日: 1999-11-05, 公開日: 2000-11-08, 最終更新日: 2023-08-09) |
| 主引用文献 | Gouet, P.,Fabry, B.,Guillet, V.,Birck, C.,Mourey, L.,Kahn, D.,Samama, J.P. Structural transitions in the FixJ receiver domain. Structure Fold.Des., 7:1517-1526, 1999 Cited by PubMed Abstract: Two-component signal transduction pathways are sophisticated phosphorelay cascades widespread in prokaryotes and also found in fungi, molds and plants. FixL/FixJ is a prototypical system responsible for the regulation of nitrogen fixation in the symbiotic bacterium Sinorhizobium meliloti. In microaerobic conditions the membrane-bound kinase FixL uses ATP to transphosphorylate a histidine residue, and the response regulator FixJ transfers the phosphoryl group from the phosphohistidine to one of its own aspartate residues in a Mg(2+)-dependent mechanism. PubMed: 10647182DOI: 10.1016/S0969-2126(00)88342-2 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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