1aih
From Proteopedia
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Revision as of 12:43, 30 October 2007
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CATALYTIC DOMAIN OF BACTERIOPHAGE HP1 INTEGRASE
Overview
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.
About this Structure
1AIH is a [Single protein] structure of sequence from [Haemophilus phage hp1] with SO4 and MG as [ligands]. Structure known Active Sites: ACA, ACB, ACC and ACD. Full crystallographic information is available from [OCA].
Reference
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
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