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5c6k

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'''Unreleased structure'''
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==Bacteriophage P2 integrase catalytic domain==
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<StructureSection load='5c6k' size='340' side='right' caption='[[5c6k]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5c6k]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C6K FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6k OCA], [http://pdbe.org/5c6k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6k RCSB], [http://www.ebi.ac.uk/pdbsum/5c6k PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/VINT_BPP2 VINT_BPP2]] Integrase is necessary for integration of the phage into the host genome by site-specific recombination.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 the structure-function relationship of several previously identified non-functional P2 integrase mutants. The DNA binding area is characterized by a large positively charged patch, harboring key residues. The structure reveals potential for large dimer flexibility, likely essential for rearrangement of DNA strands upon integration and excision of the phage DNA.
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The entry 5c6k is ON HOLD
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Crystal structure of the bacteriophage P2 integrase catalytic domain.,Skaar K, Claesson M, Odegrip R, Hogbom M, Haggard-Ljungquist E, Stenmark P FEBS Lett. 2015 Oct 8. pii: S0014-5793(15)00875-3. doi:, 10.1016/j.febslet.2015.09.026. PMID:26453836<ref>PMID:26453836</ref>
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Authors: Skaar, K., Claesson, M., Odegrip, R., Eriksson, J., Hogbom, M., Haggard-Ljungquist, E., Stenmark, P.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Bacteriophage P2 integrase catalytic domain
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<div class="pdbe-citations 5c6k" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Claesson, M]]
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[[Category: Eriksson, J]]
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[[Category: Haggard-Ljungquist, E]]
[[Category: Hogbom, M]]
[[Category: Hogbom, M]]
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[[Category: Eriksson, J]]
 
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[[Category: Claesson, M]]
 
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[[Category: Stenmark, P]]
 
[[Category: Odegrip, R]]
[[Category: Odegrip, R]]
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[[Category: Haggard-Ljungquist, E]]
 
[[Category: Skaar, K]]
[[Category: Skaar, K]]
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[[Category: Stenmark, P]]
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[[Category: Hydrolase]]
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[[Category: Integrase]]
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[[Category: Integration]]
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[[Category: Site-specific recombination]]
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[[Category: Tyrosine recombinase]]

Revision as of 05:23, 22 October 2015

Bacteriophage P2 integrase catalytic domain

5c6k, resolution 1.90Å

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