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The uteroglobin fold.

I Callebaut1, A Poupon, R Bally

  • 1Systèmes Moléculaires et Biologie Structurale, Laboratoire de Minéralogie-Cristallographie Paris (LMCP), CNRS UMR 7590, Universités Paris 6 et Paris 7, Case 115, 4 Place Jussieu, 75252 Paris, France. Isabelle.Callebaut@lmcp.jussieu.fr

Annals of the New York Academy of Sciences
|February 24, 2001
PubMed
Summary

Uteroglobin (UTG) and similar protein folds act as "geodes" to bind hydrophobic molecules. New crystal data and molecular dynamics reveal potential new pathways for ligand entry into the UTG internal cavity.

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Area of Science:

  • Protein structure and evolution
  • Biochemistry
  • Structural biology

Background:

  • Uteroglobin (UTG) is a homodimeric protein with a hydrophobic cavity for ligand binding.
  • The UTG fold is observed in the UTG/CC10 family and the cap domain of Xanthobacter autotrophicus haloalkane dehalogenase.

Purpose of the Study:

  • To investigate the prevalence of the UTG fold in other protein families.
  • To present new structural data for oxidized rabbit UTG.
  • To explore ligand binding mechanisms using molecular dynamics.

Main Methods:

  • Sequence and structure analysis
  • X-ray crystallography
  • Molecular dynamics simulations

Main Results:

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  • The UTG fold is adopted by several cap domains within the alpha/beta hydrolase family, functioning as a "geode" structure.
  • New crystal form data for oxidized rabbit UTG were obtained.
  • Molecular dynamics simulations suggest an alternative ligand entry pathway into the UTG internal cavity.

Conclusions:

  • The UTG fold is a versatile structural motif found across various protein families for sequestering hydrophobic molecules.
  • Further structural and dynamic studies of UTG provide insights into its ligand-binding mechanisms.