3W15

Structure of peroxisomal targeting signal 2 (PTS2) of Saccharomyces cerevisiae 3-ketoacyl-CoA thiolase in complex with Pex7p and Pex21p

3W15 の概要

• エントリーDOI: 10.2210/pdb3w15/pdb
• 分子名称: Peroxisomal targeting signal 2 receptor, Peroxisomal membrane protein PEX21, 3-ketoacyl-CoA thiolase, peroxisomal, Maltose-binding periplasmic protein, ... (6 entities in total)
• 機能のキーワード: beta-propeller, targeting signal recognition, cytosol, peroxisome, protein transport
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Cytoplasm: P39108 P50091; Periplasm: P0AEX9
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 96131.38

構造登録者

Pan, D.,Nakatsu, T.,Kato, H. (登録日: 2012-11-06, 公開日: 2013-07-03, 最終更新日: 2017-08-16)

主引用文献

Pan, D.,Nakatsu, T.,Kato, H.
Crystal structure of peroxisomal targeting signal-2 bound to its receptor complex Pex7p-Pex21p
Nat.Struct.Mol.Biol., 20:987-993, 2013

PubMed Abstract: Appropriate targeting of matrix proteins to peroxisomes is mainly directed by two types of peroxisomal targeting signals, PTS1 and PTS2. Although the basis of PTS1 recognition has been revealed by structural studies, that of PTS2 recognition remains elusive. Here we present the crystal structure of a heterotrimeric PTS2-recognition complex from Saccharomyces cerevisiae, containing Pex7p, the C-terminal region of Pex21p and the PTS2 of the peroxisomal 3-ketoacyl-CoA thiolase. Pex7p forms a β-propeller structure and provides a platform for cooperative interactions with both the amphipathic PTS2 helix and Pex21p. The C-terminal region of Pex21p directly covers the hydrophobic surfaces of both Pex7p and PTS2, and the resulting hydrophobic core is the primary determinant of stable complex formation. Together with in vivo and in vitro functional assays of Pex7p and Pex21p variants, our findings reveal the molecular mechanism of PTS2 recognition.

PubMed: 23812376
DOI: 10.1038/nsmb.2618

実験手法

X-RAY DIFFRACTION (1.8 Å)