1AIH

CATALYTIC DOMAIN OF BACTERIOPHAGE HP1 INTEGRASE

1AIH の概要

• エントリーDOI: 10.2210/pdb1aih/pdb
• 分子名称: HP1 INTEGRASE, SULFATE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: dna integration, recombination
• 由来する生物種: Haemophilus phage HP1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 78719.28

構造登録者

Hickman, A.B.,Waninger, S.,Scocca, J.J.,Dyda, F. (登録日: 1997-04-17, 公開日: 1997-08-20, 最終更新日: 2024-02-07)

主引用文献

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

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: 9108478
DOI: 10.1016/S0092-8674(00)80202-0

実験手法

X-RAY DIFFRACTION (2.5 Å)