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...
Gespeichert in:
| Hauptverfasser: | , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
03 March 2010
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| In: |
FEBS letters
Year: 2010, Jahrgang: 584, Heft: 8, Pages: 1509-1514 |
| ISSN: | 1873-3468 |
| DOI: | 10.1016/j.febslet.2010.02.070 |
| Online-Zugang: | 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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| Verfasserangaben: | Gunes Bozkurt, Klemens Wild, Stefan Amlacher, Ed Hurt, Bernhard Dobberstein, Irmgard Sinning |
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| 520 | |a 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. | ||
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