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

E. coli trp repressor forms a domain-swapped array in aqueous alcohol.

Catherine L Lawson1, Brian Benoff, Tatyana Berger

  • 1Rutgers University, Department of Chemistry and Chemical Biology, 610 Taylor Road, Piscataway, NJ 08854, USA. cathy.lawson@rutgers.edu

Structure (London, England : 1993)
|July 28, 2004
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

New targets and procedures for validating the valence geometry of nucleic acid structures.

Nucleic acids research·2026
Same author

An MD View of Ligand Binding.

Molecules (Basel, Switzerland)·2025
Same author

IHMValidation: Assessment of Integrative Structure Models Deposited to the Protein Data Bank.

Journal of molecular biology·2025
Same author

RCSB Protein Data Bank: Delivering integrative structures alongside experimental structures and computed structure models.

Nucleic acids research·2025
Same author

RNAproDB: A Webserver and Interactive Database for Analyzing Protein-RNA Interactions.

Journal of molecular biology·2025
Same author

PDB-IHM: A System for Deposition, Curation, Validation, and Dissemination of Integrative Structures.

Journal of molecular biology·2025
Same journal

Structure of Perinereis linea erythrocruorin reveals a compact extracellular globin megacomplex.

Structure (London, England : 1993)·2026
Same journal

Meet the author: Stephen Brohawn.

Structure (London, England : 1993)·2026
Same journal

Tetraspanins bring Norrin into focus: Structural insights into ligand-specific Wnt signaling.

Structure (London, England : 1993)·2026
Same journal

Uncovering subtype-selective activation of the K<sub>Ca</sub>3.1 channel by SKA-111.

Structure (London, England : 1993)·2026
Same journal

Identification and structure determination of a type III-Bv CRISPR complex that post-translationally modifies an associated toxin.

Structure (London, England : 1993)·2026
Same journal

Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states.

Structure (London, England : 1993)·2026
See all related articles

The E. coli trp repressor (trpR) protein undergoes significant structural changes in isopropanol, forming a unique 3D domain-swapped array. This alters its DNA-binding properties and self-association in solution.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • The E. coli trp repressor (trpR) is a key regulator of tryptophan biosynthesis.
  • It functions as a homodimer, utilizing helix-turn-helix (HTH) motifs to bind palindromic DNA sequences.
  • Flexible N-terminal arms facilitate interactions between trp repressor dimers bound to adjacent DNA sites.

Purpose of the Study:

  • To investigate the structural and self-association properties of the E. coli trp repressor (trpR) in the presence of isopropanol.
  • To elucidate the conformational changes induced by isopropanol crystallization.

Main Methods:

  • X-ray crystallography at 2.5 A resolution.
  • Small angle X-ray scattering (SAXS) measurements in solution.

Related Experiment Videos

Main Results:

  • Crystallization in 30% isopropanol induced a significant conformational rearrangement of trp repressor's HTH motifs and N-terminal arms.
  • The protein adopted an unusual ordered 3D domain-swapped supramolecular array.
  • SAXS data indicated that isopropanol fundamentally altered the self-association properties of trp repressor in solution.

Conclusions:

  • Isopropanol induces major structural reorganization in E. coli trp repressor, leading to domain swapping and altered self-association.
  • These findings reveal novel quaternary structures and solution behaviors of trp repressor under specific solvent conditions.