1F6B

CRYSTAL STRUCTURE OF SAR1-GDP COMPLEX

Summary for 1F6B

• Entry DOI: 10.2210/pdb1f6b/pdb
• Related: 1hur 1q21 1rrg
• Descriptor: SAR1, MAGNESIUM ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: gtpases, n-terminal helix, mg-containing complex, protein transport
• Biological source: Cricetulus griseus (Chinese hamster)
• Cellular location: Endoplasmic reticulum membrane; Peripheral membrane protein: Q9QVY3
• Total number of polymer chains: 2
• Total formula weight: 46287.05

Authors

Huang, M.,Wilson, I.A.,Balch, W.E. (deposition date: 2000-06-21, release date: 2002-01-09, Last modification date: 2024-02-07)

Primary citation

Huang, M.,Weissman, J.T.,Beraud-Dufour, S.,Luan, P.,Wang, C.,Chen, W.,Aridor, M.,Wilson, I.A.,Balch, W.E.
Crystal structure of Sar1-GDP at 1.7 A resolution and the role of the NH2 terminus in ER export.
J.Cell Biol., 155:937-948, 2001

PubMed Abstract: 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.

PubMed: 11739406
DOI: 10.1083/jcb.200106039

Experimental method

X-RAY DIFFRACTION (1.7 Å)