PMID:15066428
| Citation |
Sam, MD, Cascio, D, Johnson, RC and Clubb, RT (2004) Crystal structure of the excisionase-DNA complex from bacteriophage lambda. J. Mol. Biol. 338:229-40 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1016/j.jmb.2004.02.053 |
| Keywords |
Amino Acid Sequence; Bacteriophage lambda/enzymology; Base Sequence; Binding Sites; Crystallography, X-Ray; DNA/chemistry; DNA/metabolism; DNA Nucleotidyltransferases/chemistry; DNA Nucleotidyltransferases/metabolism; Models, Molecular; Molecular Sequence Data; Molecular Structure; Nucleic Acid Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Viral Proteins |
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