The structure of Get4 reveals an alpha-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis
Authors: Bozkurt G, Wild K, Amlacher S, Hurt E, Dobberstein B, Sinning I
CellNetworks People: Dobberstein Bernhard, Hurt Ed, Sinning Irmgard
Journal: FEBS Lett. 2010 Apr 16;584(8):1509-14

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.