1AIH
CATALYTIC DOMAIN OF BACTERIOPHAGE HP1 INTEGRASE
Summary for 1AIH
| Entry DOI | 10.2210/pdb1aih/pdb |
| Descriptor | HP1 INTEGRASE, SULFATE ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | dna integration, recombination |
| Biological source | Haemophilus phage HP1 |
| Total number of polymer chains | 4 |
| Total formula weight | 78719.28 |
| Authors | Hickman, A.B.,Waninger, S.,Scocca, J.J.,Dyda, F. (deposition date: 1997-04-17, release date: 1997-08-20, Last modification date: 2024-02-07) |
| Primary citation | Hickman, A.B.,Waninger, S.,Scocca, J.J.,Dyda, F. Molecular organization in site-specific recombination: the catalytic domain of bacteriophage HP1 integrase at 2.7 A resolution. Cell(Cambridge,Mass.), 89:227-237, 1997 Cited by PubMed Abstract: HP1 integrase promotes site-specific recombination of the HP1 genome into that of Haemophilus influenzae. The isolated C-terminal domain (residues 165-337) of the protein interacts with the recombination site and contains the four catalytic residues conserved in the integrase family. This domain represents a novel fold consisting principally of well-packed alpha helices, a surface beta sheet, and an ordered 17-residue C-terminal tail. The conserved triad of basic residues and the active-site tyrosine are contributed by a single monomer and occupy fixed positions in a defined active-site cleft. Dimers are formed by mutual interactions of the tail of one monomer with an adjacent monomer; this orients active-site clefts antiparallel to each other. PubMed: 9108478DOI: 10.1016/S0092-8674(00)80202-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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