1rh6: Difference between revisions

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[[Image:1rh6.gif|left|200px]]
{{Seed}}
[[Image:1rh6.png|left|200px]]


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{{STRUCTURE_1rh6|  PDB=1rh6  |  SCENE=  }}  
{{STRUCTURE_1rh6|  PDB=1rh6  |  SCENE=  }}  


'''Bacteriophage Lambda Excisionase (Xis)-DNA Complex'''
===Bacteriophage Lambda Excisionase (Xis)-DNA Complex===




==Overview==
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The excisionase (Xis) protein from bacteriophage lambda is the best characterized member of a large family of recombination directionality factors that control integrase-mediated DNA rearrangements. It triggers phage excision by cooperatively binding to sites X1 and X2 within the phage, bending DNA significantly and recruiting the phage-encoded integrase (Int) protein to site P2. We have determined the co-crystal structure of Xis with its X2 DNA-binding site at 1.7A resolution. Xis forms a unique winged-helix motif that interacts with the major and minor grooves of its binding site using an alpha-helix and an ordered beta-hairpin (wing), respectively. Recognition is achieved through an elaborate water-mediated hydrogen-bonding network at the major groove interface, while the preformed hairpin forms largely non-specific interactions with the minor groove. The structure of the complex provides insights into how Xis recruits Int cooperatively, and suggests a plausible mechanism by which it may distort longer DNA fragments significantly. It reveals a surface on the protein that is likely to mediate Xis-Xis interactions required for its cooperative binding to DNA.
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{{ABSTRACT_PUBMED_15066428}}


==About this Structure==
==About this Structure==
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[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
[[Category: Site-specific dna recombination]]
[[Category: Site-specific dna recombination]]
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