The structure of Get4 reveals an alpha-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 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.
Bozkurt
Gunes
G
Heidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
Wild
Klemens
K
Amlacher
Stefan
S
Hurt
Ed
E
Dobberstein
Bernhard
B
Sinning
Irmgard
I
D000222:Adaptation, Physiological; D000595:Amino Acid Sequence; D001665:Binding Sites; D002597:Chaetomium / Q000378:metabolism*; D017124:Conserved Sequence; D005656:Fungal Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D014176:Protein Biosynthesis; D011487:Protein Conformation; D017510:Protein Folding
D005656:Fungal Proteins