1BCO
BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN
1BCO の概要
| エントリーDOI | 10.2210/pdb1bco/pdb |
| 分子名称 | BACTERIOPHAGE MU TRANSPOSASE (2 entities in total) |
| 機能のキーワード | polynucleotidyl transferase, dna binding, endonuclease, integrase, transposase |
| 由来する生物種 | Enterobacteria phage Mu |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 36888.08 |
| 構造登録者 | |
| 主引用文献 | Rice, P.,Mizuuchi, K. Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell(Cambridge,Mass.), 82:209-220, 1995 Cited by PubMed Abstract: The crystal structure of the core domain of bacteriophage Mu transposase, MuA, has been determined at 2.4 A resolution. The first of two subdomains contains the active site and, despite very limited sequence homology, exhibits a striking similarity to the core domain of HIV-1 integrase, which carries out a similar set of biochemical reactions. It also exhibits more limited similarity to other nucleases, RNase H and RuvC. The second, a beta barrel, connects to the first subdomain through several contacts. Three independent determinations of the monomer structure from two crystal forms all show the active site held in a similar, apparently inactive configuration. The enzymatic activity of MuA is known to be activated by formation of a DNA-bound tetramer of the protein. We propose that the connections between the two subdomains may be involved in the cross-talk between the active site and the other domains of the transposase that controls the activity of the protein. PubMed: 7628012DOI: 10.1016/0092-8674(95)90308-9 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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