3ETV

Crystal structure of a Tip20p-Dsl1p fusion protein

3ETV の概要

• エントリーDOI: 10.2210/pdb3etv/pdb
• 関連するPDBエントリー: 3ETU
• 分子名称: Protein transport protein TIP20, Protein transport protein DSL1 chimera (2 entities in total)
• 機能のキーワード: tip20p-dsl1p complex, endoplasmic reticulum, er-golgi transport, membrane, phosphoprotein, protein transport, transport, transport protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Endoplasmic reticulum membrane ; Peripheral membrane protein : P53847
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40313.68

構造登録者

Ren, Y.,Jeffrey, P.D.,Hughson, F.M. (登録日: 2008-10-08, 公開日: 2009-01-20, 最終更新日: 2023-09-06)

主引用文献

Tripathi, A.,Ren, Y.,Jeffrey, P.D.,Hughson, F.M.
Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex.
Nat.Struct.Mol.Biol., 16:114-123, 2009

PubMed Abstract: Multisubunit tethering complexes are essential for intracellular trafficking and have been proposed to mediate the initial interaction between vesicles and the membranes with which they fuse. Here we report initial structural characterization of the Dsl1p complex, whose three subunits are essential for trafficking from the Golgi apparatus to the endoplasmic reticulum (ER). Crystal structures reveal that two of the three subunits, Tip20p and Dsl1p, resemble known subunits of the exocyst complex, establishing a structural connection among several multisubunit tethering complexes and implying that many of their subunits are derived from a common progenitor. We show, moreover, that Tip20p and Dsl1p interact directly via N-terminal alpha-helices. Finally, we establish that different Dsl1p complex subunits bind independently to different ER SNARE proteins. Our results map out two alternative protein-interaction networks capable of tethering COPI-coated vesicles, via the Dsl1p complex, to ER membranes.

PubMed: 19151722
DOI: 10.1038/nsmb.1548

実験手法

X-RAY DIFFRACTION (1.94 Å)