The structure of Get4 reveals an alpha-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis

FEBS Lett. 2010 Apr 16;584(8):1509-14. doi: 10.1016/j.febslet.2010.02.070. Epub 2010 Mar 3.

Abstract

Tail-anchored proteins play important roles in protein translocation, membrane fusion and apoptosis. They are targeted to the endoplasmic reticulum membrane via the guided-entry of tail-anchored proteins (Get) pathway. We present the 2A crystal structure of Get4 which participates in early steps of the Get pathway. The structure shows an alpha-solenoid fold with particular deviations from the regular pairwise arrangement of alpha-helices. A conserved hydrophobic groove accommodates the flexible C-terminal region in trans. The structural organization of the Get4 helical hairpin motifs provides a scaffold for protein-protein interactions in the Get pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological
  • Amino Acid Sequence
  • Binding Sites
  • Chaetomium / metabolism*
  • Conserved Sequence
  • Fungal Proteins / biosynthesis
  • Fungal Proteins / chemistry*
  • Fungal Proteins / metabolism*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Biosynthesis*
  • Protein Conformation
  • Protein Folding*

Substances

  • Fungal Proteins