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Related Experiment Videos

An alpha to beta conformational switch in EF-Tu

K Abel1, M D Yoder, R Hilgenfeld

  • 1Department of Biochemistry, University of California, Riverside, CA 92521-0129, USA.

Structure (London, England : 1993)
|October 15, 1996
PubMed
Summary
This summary is machine-generated.

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The bacterial elongation factor EF-Tu's GDP-bound structure reveals an ordered Switch I region, similar to other GTPases. This alpha-helix to beta-sheet conformational change may be a key activation mechanism for protein families.

Area of Science:

  • Structural biology
  • Molecular biology
  • Biochemistry

Background:

  • Bacterial elongation factor EF-Tu (Elongation Factor Thermounstable) is crucial for protein synthesis, interacting with aminoacyl-tRNAs and ribosomes.
  • EF-Tu belongs to the GTPase superfamily, with its conformation regulated by guanine nucleotide binding (GTP or GDP).

Purpose of the Study:

  • To determine the three-dimensional structure of the bacterial elongation factor EF-Tu complexed with GDP.
  • To investigate the structural impact of the antibiotic GE2270 A on EF-Tu-GDP.
  • To elucidate the conformational changes associated with nucleotide binding in EF-Tu.

Main Methods:

  • Crystallization of intact Escherichia coli EF-Tu complexed with GDP in the presence of antibiotic GE2270 A.
  • X-ray diffraction analysis to solve the three-dimensional structure.

Related Experiment Videos

  • Refinement of the crystal structure to a resolution of 2.5 Å.

    • Main Results:

    • The crystal structure of EF-Tu-GDP was determined at 2.5 Å resolution.
    • The antibiotic GE2270 A binding site could not be localized within the determined structure.
    • The structure of EF-Tu-GDP was found to be nearly identical to a trypsin-modified form, validating the structural integrity.

    Conclusions:

    • The determined EF-Tu-GDP structure presents the first view of an ordered Switch I region in this protein.
    • The Switch I region exhibits similarities to those in other GDP-bound GTPases like Ran and ADP-ribosylation factor-1.
    • A significant conformational change, an alpha-helix to beta-sheet transition in a six-amino acid segment, occurs between the GTP and GDP forms of EF-Tu, potentially representing a conserved activation mechanism.