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

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 2 Å crystal structure of Get4 which participates in early steps o...

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Bibliographic Details
Main Authors: Bozkurt, Gunes (Author) , Wild, Klemens (Author) , Amlacher, Stefan (Author) , Hurt, Ed (Author) , Dobberstein, Bernhard (Author) , Sinning, Irmgard (Author)
Format: Article (Journal)
Language:English
Published: 03 March 2010
In: FEBS letters
Year: 2010, Volume: 584, Issue: 8, Pages: 1509-1514
ISSN:1873-3468
DOI:10.1016/j.febslet.2010.02.070
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.febslet.2010.02.070
Verlag, lizenzpflichtig, Volltext: https://onlinelibrary.wiley.com/doi/abs/10.1016/j.febslet.2010.02.070
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Author Notes:Gunes Bozkurt, Klemens Wild, Stefan Amlacher, Ed Hurt, Bernhard Dobberstein, Irmgard Sinning
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Summary: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 2 Å crystal structure of Get4 which participates in early steps of the Get pathway. The structure shows an α-solenoid fold with particular deviations from the regular pairwise arrangement of α-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.
Item Description:Gesehen am 15.02.2023
Physical Description:Online Resource
ISSN:1873-3468
DOI:10.1016/j.febslet.2010.02.070

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