3CUE

Crystal structure of a TRAPP subassembly activating the Rab Ypt1p

3CUE の概要

• エントリーDOI: 10.2210/pdb3cue/pdb
• 分子名称: Transport protein particle 23 kDa subunit, Transport protein particle 31 kDa subunit, Transport protein particle 18 kDa subunit, ... (6 entities in total)
• 機能のキーワード: membrane traffic, gef, tethering complex, rab activation, guanine nucleotide exchange factor, endoplasmic reticulum, er-golgi transport, golgi apparatus, transport, lipoprotein, palmitate, gtp-binding, nucleotide-binding, phosphoprotein, prenylation, protein transport
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Golgi apparatus, cis-Golgi network: Q03784 Q03337 Q03630 P36149; Endoplasmic reticulum membrane; Peripheral membrane protein: P01123
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 571601.47

構造登録者

Cai, Y.,Reinisch, K.M. (登録日: 2008-04-16, 公開日: 2008-07-08, 最終更新日: 2024-10-16)

主引用文献

Cai, Y.,Chin, H.F.,Lazarova, D.,Menon, S.,Fu, C.,Cai, H.,Sclafani, A.,Rodgers, D.W.,De La Cruz, E.M.,Ferro-Novick, S.,Reinisch, K.M.
The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes.
Cell(Cambridge,Mass.), 133:1202-1213, 2008

PubMed Abstract: The multimeric membrane-tethering complexes TRAPPI and TRAPPII share seven subunits, of which four (Bet3p, Bet5p, Trs23p, and Trs31p) are minimally needed to activate the Rab GTPase Ypt1p in an event preceding membrane fusion. Here, we present the structure of a heteropentameric TRAPPI assembly complexed with Ypt1p. We propose that TRAPPI facilitates nucleotide exchange primarily by stabilizing the nucleotide-binding pocket of Ypt1p in an open, solvent-accessible form. Bet3p, Bet5p, and Trs23p interact directly with Ypt1p to stabilize this form, while the C terminus of Bet3p invades the pocket to participate in its remodeling. The Trs31p subunit does not interact directly with the GTPase but allosterically regulates the TRAPPI interface with Ypt1p. Our findings imply that TRAPPII activates Ypt1p by an identical mechanism. This view of a multimeric membrane-tethering assembly complexed with a Rab provides a framework for understanding events preceding membrane fusion at the molecular level.

PubMed: 18585354
DOI: 10.1016/j.cell.2008.04.049

実験手法

X-RAY DIFFRACTION (3.7 Å)