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Related Experiment Videos

Engineering alternative beta-turn types in staphylococcal nuclease

T R Hynes1, A Hodel, R O Fox

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520.

Biochemistry
|May 3, 1994
PubMed
Summary
This summary is machine-generated.

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Altering staphylococcal nuclease

Area of Science:

  • Protein crystallography
  • Structural biology
  • Biochemistry

Background:

  • Staphylococcal nuclease contains a type VIa beta-turn with a cis peptide bond.
  • Beta-turns are crucial structural motifs in proteins, influencing overall conformation and function.

Purpose of the Study:

  • To investigate how single amino acid substitutions in a specific beta-turn affect protein backbone conformation.
  • To explore the relationship between amino acid sequence and beta-turn type in staphylococcal nuclease.

Main Methods:

  • Refined crystal structures of three staphylococcal nuclease point mutants.
  • Utilized X-ray crystallography to determine detailed protein structures.

Main Results:

  • Mutations P117T, P117G, and P117A induced new beta-turn conformations (type I and I').

Related Experiment Videos

  • Observed significant backbone conformational changes, reorienting side chains into the nucleotide binding pocket.
  • Results align with sequence-conformation correlations, with P117A as a notable exception.

    • Conclusions:

    • Single residue changes can dramatically alter protein backbone conformation and surface structure.
    • Demonstrates potential for protein engineering to modify enzyme function by altering side chain positioning.
    • Provides crystallographic insights into sequence-dependent beta-turn conformations within a conserved protein fold.