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1aih
From Proteopedia
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'''CATALYTIC DOMAIN OF BACTERIOPHAGE HP1 INTEGRASE''' | '''CATALYTIC DOMAIN OF BACTERIOPHAGE HP1 INTEGRASE''' | ||
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[[Category: Scocca, J J.]] | [[Category: Scocca, J J.]] | ||
[[Category: Waninger, S.]] | [[Category: Waninger, S.]] | ||
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| - | [[Category: | + | [[Category: Recombination]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:18:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:18, 2 May 2008
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. 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 Fri May 2 10:18:41 2008
