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

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

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1
Heidelberg University Biochemistry Center (BZH), Heidelberg, Germany.

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.

PMID:
20206626
DOI:
10.1016/j.febslet.2010.02.070
[Indexed for MEDLINE]
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