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Related Experiment Videos

Secondary structure switching in Cro protein evolution.

Tracey Newlove1, Jay H Konieczka, Matthew H J Cordes

  • 1Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, AZ 85701 USA.

Structure (London, England : 1993)
|April 6, 2004
PubMed
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The solution structure of bacteriophage P22 Cro protein reveals an all-alpha fold, suggesting an evolutionary alpha-to-beta structure switch in Cro evolution. This contrasts with lambda Cro

Area of Science:

  • Structural biology
  • Molecular evolution
  • Virology

Background:

  • Cro proteins are key regulators in bacteriophage gene expression.
  • Lambda Cro and P22 Cro are homologous but exhibit distinct protein folds.
  • Understanding their structural evolution provides insights into protein adaptation.

Purpose of the Study:

  • To determine the solution structure of the Cro protein from bacteriophage P22.
  • To compare the structure of P22 Cro with that of lambda Cro.
  • To elucidate the evolutionary pathway of Cro protein folds.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy for structure determination.
  • Sequence and structural homology analysis using PSI-BLAST and transitive homology.

Related Experiment Videos

  • Comparative analysis of secondary structure elements.

    • Main Results:

    • The solution structure of P22 Cro reveals an all-alpha helical fold.
    • P22 Cro and lambda Cro share a homologous N-terminal three-alpha helix fragment.
    • P22 Cro's C-terminus is helical, while lambda Cro's is a beta hairpin, indicating a secondary structure switch.

    Conclusions:

    • The all-alpha fold of P22 Cro is likely ancestral, also found in ancient cI proteins.
    • Lambda Cro's alpha+beta fold likely evolved from an all-alpha ancestor via homologous secondary structure switching.
    • This suggests a mechanism of protein fold evolution involving conserved homology and structural rearrangement.