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Crystal structure o...
Crystal structure of the bacteriophage P2 integrase catalytic domain
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- Skaar, Karin (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Claesson, Magnus (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Odegrip, Richard (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Högbom, Magnus (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Haggård-Ljungquist, Elisabeth (author)
- Stockholms universitet,Institutionen för molekylär biovetenskap, Wenner-Grens institut
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- Stenmark, Pål (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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(creator_code:org_t)
- 2015-10-08
- 2015
- English.
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In: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 589:23, s. 3556-3563
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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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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