3A58

Crystal structure of Sec3p - Rho1p complex from Saccharomyces cerevisiae

3A58 の概要

• エントリーDOI: 10.2210/pdb3a58/pdb
• 分子名称: Exocyst complex component SEC3, GTP-binding protein RHO1, PHOSPHATE ION, ... (6 entities in total)
• 機能のキーワード: protein complex, ph domain, gtpase, membrane traffic, exocytosis, phosphoprotein, protein transport, transport, cell membrane, endosome, gtp-binding, lipoprotein, membrane, methylation, nucleotide-binding, peroxisome, prenylation, protein transport-exocytosis complex, protein transport/exocytosis
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Cell membrane; Lipid-anchor: P06780
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 173404.39

構造登録者

Yamashita, M.,Sato, Y.,Yamagata, A.,Mimura, H.,Yoshikawa, A.,Fukai, S. (登録日: 2009-08-03, 公開日: 2010-01-12, 最終更新日: 2024-10-23)

主引用文献

Yamashita, M.,Kurokawa, K.,Sato, Y.,Yamagata, A.,Mimura, H.,Yoshikawa, A.,Sato, K.,Nakano, A.,Fukai, S.
Structural basis for the Rho- and phosphoinositide-dependent localization of the exocyst subunit Sec3
Nat.Struct.Mol.Biol., 17:180-186, 2010

PubMed Abstract: The exocyst complex is a hetero-octameric protein complex that functions during cell polarization by tethering the secretory vesicle to the target membrane. The yeast exocyst subunit Sec3 binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)) and the small GTPases Rho1 and Cdc42 via its N-terminal domain (Sec3-N), and these interactions target Sec3 to the plasma membrane. Here we report the crystal structure of the Sec3-N in complex with Rho1 at 2.6-A resolution. Sec3-N adopts a pleckstrin homology (PH) fold, despite having no detectable sequence homology with other PH domains of known structure. Clusters of conserved basic residues constitute a positively charged cleft, which was identified as a binding site for PtdIns(4,5)P(2). Residues Phe77, Ile115 and Leu131 of Sec3 bind to an extended hydrophobic surface formed around switch regions I and II of Rho1. To our knowledge, these are the first structural insights into how an exocyst subunit might interact with both protein and phospholipid factors on the target membrane.

PubMed: 20062059
DOI: 10.1038/nsmb.1722

実験手法

X-RAY DIFFRACTION (2.6 Å)