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| [[Image:1rh6.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1rh6| PDB=1rh6 | SCENE= }} | | {{STRUCTURE_1rh6| PDB=1rh6 | SCENE= }} |
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| '''Bacteriophage Lambda Excisionase (Xis)-DNA Complex'''
| | ===Bacteriophage Lambda Excisionase (Xis)-DNA Complex=== |
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| ==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. | | The line below this paragraph, {{ABSTRACT_PUBMED_15066428}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15066428 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15066428}} |
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| ==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]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:29:40 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:45:53 2008'' |