1AA3
C-TERMINAL DOMAIN OF THE E. COLI RECA, NMR, MINIMIZED AVERAGE STRUCTURE
1AA3 の概要
| エントリーDOI | 10.2210/pdb1aa3/pdb |
| 分子名称 | RECA (1 entity in total) |
| 機能のキーワード | double-stranded dna binding domain, riken structural genomics/proteomics initiative, rsgi, structural genomics |
| 由来する生物種 | Escherichia coli |
| 細胞内の位置 | Cytoplasm: P0A7G6 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 7108.13 |
| 構造登録者 | Aihara, H.,Ito, Y.,Kurumizaka, H.,Terada, T.,Yokoyama, S.,Shibata, T.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 1997-01-22, 公開日: 1997-07-23, 最終更新日: 2024-04-10) |
| 主引用文献 | Aihara, H.,Ito, Y.,Kurumizaka, H.,Terada, T.,Yokoyama, S.,Shibata, T. An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing. J.Mol.Biol., 274:213-221, 1997 Cited by PubMed Abstract: RecA protein and its homologs catalyze homologous pairing of dsDNA and ssDNA, a critical reaction in homologous genetic recombination in various organisms from a virus, microbes to higher eukaryotes. In this reaction, RecA protein forms a nucleoprotein filament on ssDNA, which in turn binds to naked dsDNA for homology search. We suggested that the C-terminal domain of RecA protein plays a role in capturing the dsDNA. Here, we isolated the C-terminal domain as a soluble form and determined the solution structure by NMR spectroscopy. The overall folding of the NMR structure agrees with that of the corresponding part of the reported crystal structure, but a remarkable difference was found in a solvent-exposed region due to intermolecular contacts in the crystal. Then, we studied the interaction between the C-terminal domain and DNA, and found that significant chemical shift changes were induced in a specific region by titration with dsDNA. SsDNA induced a much smaller chemical shift perturbation. The difference of DNA concentrations to give the half-saturation of the chemical shift change showed a higher affinity of the C-terminal region toward dsDNA. Combined with our previous results, these provide direct evidence that the defined region in the C-terminal domain furnishes a binding surface for DNA. PubMed: 9398528DOI: 10.1006/jmbi.1997.1403 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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