5C6K
Bacteriophage P2 integrase catalytic domain
5C6K の概要
エントリーDOI | 10.2210/pdb5c6k/pdb |
分子名称 | Integrase (2 entities in total) |
機能のキーワード | integrase, tyrosine recombinase, integration, site-specific recombination, hydrolase |
由来する生物種 | Enterobacteria phage P2 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 66052.05 |
構造登録者 | Skaar, K.,Claesson, M.,Odegrip, R.,Eriksson, J.,Hogbom, M.,Haggard-Ljungquist, E.,Stenmark, P. (登録日: 2015-06-23, 公開日: 2015-10-21, 最終更新日: 2024-01-10) |
主引用文献 | Skaar, K.,Claesson, M.,Odegrip, R.,Hogbom, M.,Haggard-Ljungquist, E.,Stenmark, P. Crystal structure of the bacteriophage P2 integrase catalytic domain. Febs Lett., 589:3556-3563, 2015 Cited by PubMed Abstract: Bacteriophage P2 is a temperate phage capable of integrating its DNA into the host genome by site-specific recombination upon lysogenization. Integration and excision of the phage genome requires P2 integrase, which performs recognition, cleavage and joining of DNA during these processes. This work presents the high-resolution crystal structure of the catalytic domain of P2 integrase, and analysis of the structure-function relationship of several previously identified non-functional P2 integrase mutants. The DNA binding area is characterized by a large positively charged patch, harboring key residues. The structure reveals potential for large dimer flexibility, likely essential for rearrangement of DNA strands upon integration and excision of the phage DNA. PubMed: 26453836DOI: 10.1016/j.febslet.2015.09.026 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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