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Crystal structure of the bacteriophage P2 integrase catalytic domain

Skaar, Karin (author)
Stockholms universitet,Institutionen för biokemi och biofysik
Claesson, Magnus (author)
Stockholms universitet,Institutionen för biokemi och biofysik
Odegrip, Richard (author)
Stockholms universitet,Institutionen för biokemi och biofysik
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Högbom, Magnus (author)
Stockholms universitet,Institutionen för biokemi och biofysik
Haggård-Ljungquist, Elisabeth (author)
Stockholms universitet,Institutionen för molekylär biovetenskap, Wenner-Grens institut
Stenmark, Pål (author)
Stockholms universitet,Institutionen för biokemi och biofysik
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 (creator_code:org_t)
2015-10-08
2015
English.
In: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 589:23, s. 3556-3563
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • Bacteriophage P2 is a temperate phage capable of integrating its DNA into the host genome by site-specific recombination upon lysogenization. Integration and excision of the phage genome requires P2 integrase, which performs recognition, cleavage and joining of DNA during these processes. This work presents the high-resolution crystal structure of the catalytic domain of P2 integrase, and analysis of several non-functional P2 integrase mutants. The DNA binding area is characterized by a large positively charged patch, harbouring key residues. The structure reveals potential for large dimer flexibility, likely essential for rearrangement of DNA strands upon integration and excision.

Subject headings

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Keyword

Bacteriophage P2
Integrase
Integration
Site-specific recombination
Tyrosine recombinase
Biochemistry
biokemi

Publication and Content Type

ref (subject category)
art (subject category)

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