1f6b
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CRYSTAL STRUCTURE OF SAR1-GDP COMPLEX
OverviewOverview
The Sar1 GTPase is an essential component of COPII vesicle coats involved, in export of cargo from the ER. We report the 1.7-A structure of Sar1 and, find that consistent with the sequence divergence of Sar1 from Arf family, GTPases, Sar1 is structurally distinct. In particular, we show that the, Sar1 NH2 terminus contains two regions: an NH2-terminal extension, containing an evolutionary conserved hydrophobic motif that facilitates, membrane recruitment and activation by the mammalian Sec12 guanine, nucleotide exchange factor, and an alpha1' amphipathic helix that, contributes to interaction with the Sec23/24 complex that is responsible, for cargo selection during ER export. We propose that the hydrophobic Sar1, NH2-terminal activation/recruitment motif, in conjunction with the alpha1', helix, mediates the initial steps in COPII coat assembly for export from, the ER.
About this StructureAbout this Structure
1F6B is a Single protein structure of sequence from Cricetulus griseus with MG, SO4 and GDP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export., Huang M, Weissman JT, Beraud-Dufour S, Luan P, Wang C, Chen W, Aridor M, Wilson IA, Balch WE, J Cell Biol. 2001 Dec 10;155(6):937-48. Epub 2001 Dec 10. PMID:11739406
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