5DOR
P2 Integrase catalytic domain in space group P21
Summary for 5DOR
| Entry DOI | 10.2210/pdb5dor/pdb |
| Related | 5C6K |
| Descriptor | Integrase, PHOSPHATE ION, ZINC ION, ... (4 entities in total) |
| Functional Keywords | tyrosine recombinase, integrase, hydrolase |
| Biological source | Enterobacteria phage P2 |
| Total number of polymer chains | 4 |
| Total formula weight | 78434.67 |
| Authors | Skaar, K.,Claesson, M.,Odegrip, R.,Haggard-Ljungquist, E.,Hogbom, M. (deposition date: 2015-09-11, release date: 2015-12-02, Last modification date: 2024-01-10) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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