1aih
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1AIH is a | + | 1AIH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_phage_hp1 Haemophilus phage hp1] with SO4 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Sites: ACA, ACB, ACC and ACD. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AIH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: recombination]] | [[Category: recombination]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:19:42 2007'' |
Revision as of 11:14, 5 November 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
Page seeded by OCA on Mon Nov 5 13:19:42 2007
