1aih

<table><tr><td colspan='2'>[[1aih]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bphp1 Bphp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1AIH FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GENBANK U24159 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10690 BPHP1])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1aih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aih OCA], [http://pdbe.org/1aih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aih RCSB], [http://www.ebi.ac.uk/pdbsum/1aih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aih ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/VINT_BPHP1 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.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:9108478</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bphp1]]

[[Category: Dyda, F]]

[[Category: Hickman, A B]]

[[Category: Scocca, J J]]

[[Category: Waninger, S]]

[[Category: Recombination]]