Structural characterisation of PinA WW domain and a comparison with other group IV WW domains, Pin1 and Ess1

Biochim Biophys Acta. 2008 Sep;1784(9):1208-14. doi: 10.1016/j.bbapap.2008.04.026. Epub 2008 May 8.

Abstract

The NMR solution structure of the PinA WW domain from Aspergillus nidulans is presented. The backbone of the PinA WW domain is composed of a triple-stranded anti-parallel beta-sheet and an alpha-helix similar to Ess1 and Pin1 without the alpha-helix linker. Large RMS deviations in Loop I were observed both from the NMR structures and molecular dynamics simulation suggest that the Loop I of PinA WW domain is flexible and solvent accessible, thus enabling it to bind the pS/pT-P motif. The WW domain in this structure are stabilised by a hydrophobic core. It is shown that the linker flexibility of PinA is restricted because of an alpha-helical structure in the linker region. The combination of NMR structural data and detailed Molecular Dynamics simulations enables a comprehensive structural and dynamic understanding of this protein.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Aspergillus nidulans / enzymology
  • Aspergillus nidulans / genetics
  • Candida albicans / enzymology
  • Candida albicans / genetics
  • Fungal Proteins / chemistry*
  • Fungal Proteins / genetics
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Molecular Sequence Data
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptidylprolyl Isomerase / chemistry*
  • Peptidylprolyl Isomerase / genetics
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Thermodynamics

Substances

  • Fungal Proteins
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Peptidylprolyl Isomerase