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The up-and-down beta-barrel proteins

J M LaLonde1, D A Bernlohr, L J Banaszak

  • 1Department of Biochemistry, University of Minnesota, St. Paul 55108.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|December 1, 1994
PubMed
Summary

The up-and-down beta-barrel protein motif is crucial for transporting hydrophobic ligands. Two families, 10-stranded and 8-stranded, bind different molecules in distinct cavities.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Science

Background:

  • The up-and-down beta-barrel is a prevalent protein folding motif.
  • This structure is essential for binding and transporting hydrophobic ligands.
  • It consists of antiparallel beta-strands with hydrogen bonds between adjacent and terminal strands.

Purpose of the Study:

  • To analyze the structural characteristics and ligand-binding properties of up-and-down beta-barrel proteins.
  • To identify and differentiate between distinct families of these protein carriers.

Main Methods:

  • Comparative analysis of known crystal structures.
  • Identification of structural variations and ligand-binding domains.

Main Results:

  • Two evolutionarily distinct families of up-and-down beta-barrels were identified: a 10-stranded intracellular type and an 8-stranded extracellular type.
  • The 10-stranded barrels feature a hydrophilic cavity for lipids (fatty acids, retinoids).
  • The 8-stranded barrels possess a hydrophobic pit for compounds like bilins and retinoids.

Conclusions:

  • The up-and-down beta-barrel motif is a fundamental structure for hydrophobic ligand transport.
  • Structural variations allow for specialized binding of diverse hydrophobic molecules.
  • This motif represents a key evolutionary solution for biological transport challenges.

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