Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

A conformational switch controls the DNA cleavage activity of lambda integrase.

Hideki Aihara1, Hyock Joo Kwon, Simone E Nunes-Düby

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.

Molecular Cell
|July 31, 2003
PubMed
Summary

Bacteriophage lambda integrase (Int) undergoes a conformational change upon DNA binding, enabling DNA cleavage. This structural shift also facilitates protein interactions, suggesting allosteric regulation of DNA recombination.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Discovery, Structural Characterization, and Preclinical Evaluation of Monoclonal Antibodies against Xylazine Poisoning.

ACS pharmacology & translational science·2026
Same author

Selective targeting of human TREX1 exonuclease by small molecule inhibitors is mediated by a conformational switch.

NAR molecular medicine·2026
Same author

Full-length structure of the anti-viral and pro-tumor DNA deaminase APOBEC3B.

bioRxiv : the preprint server for biology·2026
Same author

Sequence-directed covalent protein-RNA linkages in a single step using engineered HUH-tags.

Nucleic acids research·2026
Same author

Structural basis for double-stranded DNA cytosine deamination by BaDTF3 and its application in mitochondrial genome editing.

Nature communications·2026
Same author

The atomic structure of human dystrophin spectrin-like repeat 24.

Acta crystallographica. Section F, Structural biology communications·2026

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Bacteriophage lambda integrase (Int) is a key enzyme in DNA recombination.
  • Tyrosine recombinases, including Int, are known for their catalytic activity in DNA rearrangements.
  • Understanding the structural basis of Int's function is crucial for deciphering DNA recombination mechanisms.

Purpose of the Study:

  • To determine the crystal structure of lambda Int complexed with a cleaved DNA substrate.
  • To elucidate the conformational changes in lambda Int upon DNA binding and cleavage.
  • To investigate the role of protein-protein interactions in regulating Int activity.

Main Methods:

  • X-ray crystallography was employed to obtain the structure of lambda Int bound to cleaved DNA.

Related Experiment Videos

  • Comparative analysis was performed between the liganded and unliganded Int structures.
  • Structural features, including domain flexibility and active site accessibility, were examined.

    • Main Results:

    • A drastic conformational change was observed in DNA-bound lambda Int, involving Tyr342 in the active site for cis-cleavage.
    • A flexible linker allows the protein to encircle the DNA, facilitating binding specificity through direct and indirect readout.
    • The C-terminal residues are exposed upon activation, mediating interactions with neighboring Int molecules.

    Conclusions:

    • The structure reveals a conformational switch mechanism that activates lambda Int for DNA cleavage.
    • Protein-protein interactions via the C-terminal tail provide a mechanism for allosteric regulation of cleavage activity.
    • These findings offer insights into the higher-order complex formation and regulatory control of lambda Int during DNA recombination.