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2B1E

The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif

2B1E の概要
エントリーDOI10.2210/pdb2b1e/pdb
関連するPDBエントリー2D2S
分子名称Exocyst complex component EXO70 (2 entities in total)
機能のキーワードtethering complex, exocyst, endocytosis-exocytosis complex, endocytosis/exocytosis
由来する生物種Saccharomyces cerevisiae (baker's yeast)
細胞内の位置Bud: P19658
タンパク質・核酸の鎖数1
化学式量合計64803.81
構造登録者
Dong, G.,Hutagalung, A.H.,Fu, C.,Novick, P.,Reinisch, K.M. (登録日: 2005-09-15, 公開日: 2005-11-01, 最終更新日: 2024-03-13)
主引用文献Dong, G.,Hutagalung, A.H.,Fu, C.,Novick, P.,Reinisch, K.M.
The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
Nat.Struct.Mol.Biol., 12:1094-1100, 2005
Cited by
PubMed Abstract: The exocyst is a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Here we present the structures of the Exo70p subunit of this complex and of the C-terminal domains of Exo84p, at 2.0-A and 2.85-A resolution, respectively. Exo70p forms a 160-A-long rod with a novel fold composed of contiguous alpha-helical bundles. The Exo84p C terminus also forms a long rod (80 A), which unexpectedly has the same fold as the Exo70p N terminus. Our structural results and our experimental observations concerning the interaction between Exo70p and other exocyst subunits or Rho3p GTPase are consistent with an architecture wherein exocyst subunits are composed of mostly helical modules strung together into long rods.
PubMed: 16249794
DOI: 10.1038/nsmb1017
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 2b1e
検証レポート(詳細版)ダウンロードをダウンロード

250059

件を2026-03-04に公開中

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