PDBsum entry 1aih

DNA integration

PDB id: 1aih

Contents

Protein chains

170 a.a. *

Ligands

SO4 ×8

Metals

_MG ×5

Waters ×152

* Residue conservation analysis

PDB id:

1aih

Name:

DNA integration

Title:

Catalytic domain of bacteriophage hp1 integrase

Structure:

Hp1 integrase. Chain: a, b, c, d. Fragment: catalytic domain, residues 168 - 337. Engineered: yes

Source:

Haemophilus phage hp1. Organism_taxid: 10690. Strain: hp1c1. Cell_line: haemophilus influenzae l10. Gene: genbank u24159. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.50Å R-factor: 0.209 R-free: 0.272

Authors:

A.B.Hickman,S.Waninger,J.J.Scocca,F.Dyda

Key ref:

A.B.Hickman et al. (1997). Molecular organization in site-specific recombination: the catalytic domain of bacteriophage HP1 integrase at 2.7 A resolution. Cell, 89, 227-237. PubMed id: 9108478 DOI: 10.1016/S0092-8674(00)80202-0

Date:

17-Apr-97 Release date: 20-Aug-97

Protein chains

P21442  (VINT_BPHC1) -  Integrase from Haemophilus phage HP1 (strain HP1c1)

Seq: 337 a.a.

Struc: 170 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class 1: E.C.2.7.7.- - ?????
• Enzyme class 2: E.C.3.1.-.-

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

DOI no: 10.1016/S0092-8674(00)80202-0

Cell 89:227-237 (1997)

PubMed id: 9108478

Molecular organization in site-specific recombination: the catalytic domain of bacteriophage HP1 integrase at 2.7 A resolution.

A.B.Hickman, S.Waninger, J.J.Scocca, F.Dyda.

ABSTRACT

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.

Selected figure(s)

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.

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.

The above figures are reprinted by permission from Cell Press: Cell (1997, 89, 227-237) copyright 1997.

Figures were selected by an automated process.