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PDBsum entry 1aih
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DNA integration
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PDB id
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1aih
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Molecular organization in site-Specific recombination: the catalytic domain of bacteriophage hp1 integrase at 2.7 a resolution.
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Authors
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A.B.Hickman,
S.Waninger,
J.J.Scocca,
F.Dyda.
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Ref.
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Cell, 1997,
89,
227-237.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1. Schematic Diagrams of the Site-Specific
Recombination Reaction(A) Site-specific recombination by
bacteriophage integrases requires two DNA substrates containing
related sequences at the site of strand exchange. For
bacteriophage HP1, the att P site is 418 bp long and, in
addition to two IHF binding sites, contains multiple integrase
binding sites: three type I sites and three type II sites that
exist as either direct or inverted repeating motifs ([18]). The
att B site is 18 bp long and contains an inverted repeat
sequence. The DNA chromosomes and their attachment sites are not
drawn to scale.(B) The steps of strand cleavage and exchange
proceed using a topoisomerase mechanism (see Introduction for
details). Adapted from Nash, 1996.
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Figure 4.
Figure 4. The Protein Fold of the Catalytic C-terminal
Domain of HP1 IntegraseMOLSCRIPT ([33]) stereo picture of the
fold of the HPC monomer. The overall fold is of a mostly α
helical globular domain from which extends an ordered 17-residue
tail.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1997,
89,
227-237)
copyright 1997.
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