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Related Experiment Videos

The UBX domain: a widespread ubiquitin-like module.

A Buchberger1, M J Howard, M Proctor

  • 1MRC Centre for Protein Engineering, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

Journal of Molecular Biology
|March 13, 2001
PubMed
Summary

The UBX domain, found in eukaryotic proteins, shares a structural fold with ubiquitin. This structural similarity suggests a ubiquitin-related function, though direct conjugation is unlikely.

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Area of Science:

  • Structural biology
  • Protein domains
  • Biochemistry

Background:

  • The UBX domain is an 80 amino acid module typically found at the carboxyl terminus of eukaryotic proteins.
  • Understanding the function of UBX domains is crucial for comprehending protein regulation and cellular processes.

Purpose of the Study:

  • To elucidate the function of UBX domains by determining the three-dimensional structure of the UBX domain from human Fas-associated factor-1 (FAF1).

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used to solve the three-dimensional structure of the FAF1 UBX domain.
  • Structural comparison with ubiquitin was performed using root-mean-square deviation (r.m.s.d.) analysis.

Main Results:

  • The FAF1 UBX domain adopts a beta-Grasp fold with a specific secondary structure organization (beta-beta-alpha-beta-beta-alpha-beta).

Related Experiment Videos

  • The UBX domain superimposes with ubiquitin (r.m.s.d. of 1.9 A), indicating a shared superfold and potential evolutionary relationship.
  • Key features for ubiquitin conjugation (carboxyl-terminal extension with double glycine motif, suitably positioned lysines) are absent, making direct conjugation unlikely.

    • Conclusions:

    • The UBX domain shares a structural fold with ubiquitin, suggesting a role in ubiquitin-related processes.
    • Most UBX domain-containing proteins belong to evolutionarily conserved families (FAF1, p47, Y33K, Rep8).
    • Direct conjugation of UBX domains to other proteins or involvement in mixed UBX-ubiquitin chains is improbable.