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

The three-dimensional structure of trp repressor.

R W Schevitz, Z Otwinowski, A Joachimiak

    Nature
    |October 6, 1985
    PubMed
    Summary
    This summary is machine-generated.

    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

    A funnel approach to enable analyses of epitope-specific human CD4 T cells specific for influenza and SARS-CoV-2.

    mBio·2026
    Same author

    Validation of 3D cryoEM single-particle reconstruction correctness and handedness with Ewald's sphere correction.

    Structural dynamics (Melville, N.Y.)·2025
    Same author

    Time-resolved β-lactam cleavage by L1 metallo-β-lactamase.

    Nature communications·2022
    Same author

    A novel signal transduction protein: Combination of solute binding and tandem PAS-like sensor domains in one polypeptide chain.

    Protein science : a publication of the Protein Society·2017
    Same author

    Databases and Archiving for CryoEM.

    Methods in enzymology·2016
    Same author

    Insight into the sporulation phosphorelay: crystal structure of the sensor domain of Bacillus subtilis histidine kinase, KinD.

    Protein science : a publication of the Protein Society·2013

    The Escherichia coli trp repressor

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Structural Biology

    Background:

    • The trp repressor regulates tryptophan biosynthesis in Escherichia coli.
    • Understanding its structure is crucial for deciphering gene regulation mechanisms.

    Purpose of the Study:

    • To determine the atomic resolution crystal structure of the Escherichia coli trp repressor.
    • To elucidate the structural basis of L-tryptophan binding and subsequent activation.

    Main Methods:

    • X-ray crystallography was employed to solve the protein structure.
    • Atomic resolution analysis was performed on the purified repressor protein.

    Main Results:

    • The dimeric trp repressor exhibits an intricate subunit interface with interlinked helices.

    Related Experiment Videos

  • L-tryptophan binding induces conformational changes, notably in the helix-turn-helix motif.
  • Structural alterations near the DNA-binding surface were observed upon L-tryptophan interaction.

    • Conclusions:

    • The study reveals a unique protein-protein interaction within the trp repressor dimer.
    • L-tryptophan allosterically modulates the repressor's DNA-binding activity through specific structural rearrangements.
    • These findings provide insights into the molecular mechanisms of transcriptional repression.