1aih
CATALYTIC DOMAIN OF BACTERIOPHAGE HP1 INTEGRASECATALYTIC DOMAIN OF BACTERIOPHAGE HP1 INTEGRASE
Structural highlights
Function[VINT_BPHP1] Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHP1 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. Molecular organization in site-specific recombination: the catalytic domain of bacteriophage HP1 integrase at 2.7 A resolution.,Hickman AB, Waninger S, Scocca JJ, Dyda F Cell. 1997 Apr 18;89(2):227-37. PMID:9108478[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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