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

YjjX: from structure "Tu" function.

Zihe Rao1

  • 1National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese Academy of Sciences, Beijing 100101, China.

Structure (London, England : 1993)
|October 12, 2005
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

Structural and functional insights into HBx-Smc6 targeting for HBV inhibition.

Cell research·2026
Same author

Architecture of surface tubular element of poxvirus.

mBio·2026
Same author

Discovery of furo[2,3-b]isoquinoline derivatives as novel Pks13 inhibitors with reduced hERG inhibition.

Bioorganic & medicinal chemistry letters·2026
Same author

Novel pyrimido[1,2-<i>a</i>]imidazole derivatives as potent Pks13-TE inhibitors: structure-based virtual screening and rational design.

RSC medicinal chemistry·2026
Same author

Direct trapping of the transport-segment DNA by the central domain of type IIA topoisomerases.

Science advances·2025
Same author

Targeting SARS-CoV-2 main protease for the discovery of a broad-spectrum COVID-19 inhibitor by intensive multi-tiered validation.

Acta pharmaceutica Sinica. B·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

Structural analysis reveals E. coli protein YjjX functions as an inosine triphosphate (ITP) hydrolase/xanthosine triphosphate (XTP) hydrolase. This suggests YjjX plays a dual role in bacterial translation regulation and response to oxidative stress.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • YjjX is a hypothetical protein in Escherichia coli.
  • Its precise biological function remains largely uncharacterized.
  • Understanding YjjX is crucial for deciphering bacterial cellular processes.

Purpose of the Study:

  • To determine the enzymatic activity of the E. coli YjjX protein.
  • To elucidate the potential biological roles of YjjX in cellular pathways.

Main Methods:

  • Structural analysis of the YjjX protein.
  • Biochemical assays to test enzymatic activity.

Main Results:

  • Structural analysis indicates YjjX possesses inosine triphosphate (ITP) hydrolase and xanthosine triphosphate (XTP) hydrolase activities.

Related Experiment Videos

  • These enzymatic activities suggest a role in nucleotide metabolism.

    • Conclusions:

    • YjjX functions as an ITPase/XTPase.
    • The protein likely plays a dual role in prokaryotic translational regulation and oxidative cell stress response.