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

NMR structure of activated CheY.

H S Cho1, S Y Lee, D Yan

  • 1Physical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Rd, Berkeley, CA, 94720, USA.

Journal of Molecular Biology
|March 25, 2000
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

[Clinical feature analysis and preliminary exploration of individualized surgical strategies in cold corneal ulcer].

[Zhonghua yan ke za zhi] Chinese journal of ophthalmology·2026
Same author

[Advances in clinical diagnosis and treatment of pythium keratitis].

[Zhonghua yan ke za zhi] Chinese journal of ophthalmology·2026
Same author

[Endotracheal mantle cell lymphoma: a case report].

Zhonghua jie he he hu xi za zhi = Zhonghua jiehe he huxi zazhi = Chinese journal of tuberculosis and respiratory diseases·2025
Same author

[Construction of a machine learning prognostic prediction model based on psoas muscle index for patients with decompensated liver cirrhosis].

Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology·2025
Same author

Transcriptomic profiling of backfat and muscle in Lijiang pigs with divergent body size across growth stages.

Scientific reports·2024
Same author

[NECRC syndrome caused by ZMYM2 gene variation in 2 cases].

Zhonghua er ke za zhi = Chinese journal of pediatrics·2024

Researchers stabilized the active state of the CheY protein, crucial for bacterial chemotaxis, using beryllofluoride. This allowed detailed structural analysis, revealing key rearrangements for protein activation.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • CheY protein acts as a response regulator in bacterial chemotaxis.
  • Phosphorylation triggers structural changes, converting CheY from inactive to active.
  • The transient nature of phosphorylated CheY hinders detailed structural studies of its active form.

Purpose of the Study:

  • To achieve persistent activation of Escherichia coli CheY.
  • To determine the structure of the active CheY protein using NMR spectroscopy.
  • To elucidate the structural mechanisms underlying CheY activation.

Main Methods:

  • Persistent activation of CheY via complexation with beryllofluoride (BeF(3)(-)).
  • Nuclear Magnetic Resonance (NMR) spectroscopy for structural determination.

Related Experiment Videos

  • Analysis of structural changes and hydrogen bond formation.

    • Main Results:

    • The structure of activated CheY was determined with high resolution (backbone r.m.s.d. of 0.58 Å).
    • A key hydrogen bond formed between Thr87 and Asp57.BeF(3)(-) stabilized the active conformation.
    • A coupled rearrangement of conserved residues (Thr87, Tyr106) and displacement of beta4/H4 were observed.

    Conclusions:

    • The study provides the first detailed structure of persistently activated CheY.
    • Stabilization via hydrogen bonding and coupled residue rearrangement are critical for CheY activation.
    • This mechanism of activation may be applicable to other receiver domains in signaling pathways.