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Related Experiment Videos

Acyl-coenzyme A binding protein (ACBP).

B B Kragelund1, J Knudsen, F M Poulsen

  • 1Carlsberg Laboratory, Department of Chemistry, Gl. Carlsberg Vej 10, DK-2500, Valby, Denmark.

Biochimica Et Biophysica Acta
|November 26, 1999
PubMed
Summary
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Acyl-coenzyme A binding proteins (ACBP) bind long-chain acyl-CoA esters. Highly conserved residues in ACBP structure are crucial for protein function, stability, and folding.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Acyl-coenzyme A binding proteins (ACBP) are conserved across eukaryotes.
  • ACBP exhibit high affinity for long-chain acyl-CoA esters.

Purpose of the Study:

  • To investigate the structural and functional roles of conserved residues in ACBP.
  • To elucidate the relationship between ACBP structure, folding, and stability.

Main Methods:

  • Biochemical mapping of ligand binding.
  • Nuclear Magnetic Resonance (NMR) spectroscopy for structural studies.
  • Site-directed mutagenesis to analyze conserved residues.

Main Results:

  • Detailed biochemical and structural data obtained for bovine ACBP apo-protein and palmitoyl-CoA complex.

Related Experiment Videos

  • Identified 21 conserved residues forming mini-cores within the four alpha-helix bundle structure.
  • Mutagenesis studies linked conserved residues to protein structure, function, folding, and stability.

    • Conclusions:

    • Conserved residues in ACBP are critical for maintaining protein integrity and function.
    • The study provides insights into the molecular mechanisms underlying ACBP stability and ligand binding.
    • Understanding these conserved elements can inform future protein engineering efforts.