1aih
From Proteopedia
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==Overview== | ==Overview== | ||
| - | HP1 integrase promotes site-specific recombination of the HP1 genome into | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dyda, F.]] | [[Category: Dyda, F.]] | ||
| - | [[Category: Hickman, A | + | [[Category: Hickman, A B.]] |
| - | [[Category: Scocca, J | + | [[Category: Scocca, J J.]] |
[[Category: Waninger, S.]] | [[Category: Waninger, S.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: recombination]] | [[Category: recombination]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:44:51 2008'' |
Revision as of 09:44, 21 February 2008
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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 and as ligands. Known structural/functional Sites: , , and . 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
Page seeded by OCA on Thu Feb 21 11:44:51 2008
