3FP4

Crystal structure of Tom71 complexed with Ssa1 C-terminal fragment

3FP4 の概要

• エントリーDOI: 10.2210/pdb3fp4/pdb
• 関連するPDBエントリー: 3FP1 3FP2 3FP3
• 分子名称: TPR repeat-containing protein YHR117W, Ssa1, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: tom71, hsp70, mitochondria, translocation, chaperone, phosphoprotein, tpr repeat, transport protein
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Mitochondrion outer membrane; Single-pass membrane protein: P38825
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62520.60

構造登録者

Li, J.,Qian, X.,Hu, J.,Sha, B. (登録日: 2009-01-03, 公開日: 2009-07-28, 最終更新日: 2023-09-06)

主引用文献

Li, J.,Qian, X.,Hu, J.,Sha, B.
Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading.
J.Biol.Chem., 284:23852-23859, 2009

PubMed Abstract: The preproteins targeted to the mitochondria are transported through the translocase of the outer membrane complex. Tom70/Tom71 is a major surface receptor of the translocase of the outer membrane complex for mitochondrial preproteins. The preproteins are escorted to Tom70/Tom71 by molecular chaperones Hsp70 and Hsp90. Here we present the high resolution crystal structures of Tom71 and the protein complexes between Tom71 and the Hsp70/Hsp90 C terminus. The crystal structures indicate that Tom70/Tom71 may exhibit two distinct states. In the closed state, the N-terminal domain of Tom70/Tom71 partially blocks the preprotein-binding pocket. In the open state, the N-terminal domain moves away, and the preprotein-binding pocket is fully exposed. The complex formation between the C-terminal EEVD motif of Hsp70/Hsp90 and Tom71 could lock Tom71 in the open state where the preprotein-binding pocket of Tom71 is ready to receive preproteins. The interactions between Hsp70/Hsp90 and Tom71 N-terminal domain generate conformational changes that may increase the volume of the preprotein-binding pocket. The complex formation of Hsp70/Hsp90 and Tom71 also generates significant domain rearrangement within Tom71, which may position the preprotein-binding pocket closer to Hsp70/Hsp90 to facilitate the preprotein transfer from the molecular chaperone to Tom71. Therefore, molecular chaperone Hsp70/Hsp90 may function to prepare the mitochondrial outer membrane receptor Tom71 for preprotein loading.

PubMed: 19581297
DOI: 10.1074/jbc.M109.023986

実験手法

X-RAY DIFFRACTION (2.14 Å)