2W84

Structure of Pex14 in complex with Pex5

2W84 の概要

• エントリーDOI: 10.2210/pdb2w84/pdb
• 関連するPDBエントリー: 1FCH 2C0L 2C0M 2J9Q 2W85
• 分子名称: PEROXISOMAL MEMBRANE PROTEIN PEX14, PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR (2 entities in total)
• 機能のキーワード: zellweger syndrome, alternative splicing, phosphoprotein, protein complex, disease mutation, peroxisome, tpr repeat, polymorphism, translocation, peroxisome biogenesis disorder, protein transport, peroxisome import, pts, receptor-cargo complex, peroxisome targeting signal
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cytoplasm: P50542
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 9716.86

構造登録者

Neufeld, C.,Filipp, F.V.,Simon, B.,Neuhaus, A.,Schueller, N.,David, C.,Kooshapur, H.,Madl, T.,Erdmann, R.,Schliebs, W.,Wilmanns, M.,Sattler, M. (登録日: 2009-01-09, 公開日: 2009-02-17, 最終更新日: 2024-05-15)

主引用文献

Neufeld, C.,Filipp, F.V.,Simon, B.,Neuhaus, A.,Schuller, N.,David, C.,Kooshapur, H.,Madl, T.,Erdmann, R.,Schliebs, W.,Wilmanns, M.,Sattler, M.
Structural basis for competitive interactions of Pex14 with the import receptors Pex5 and Pex19.
EMBO J., 28:745-754, 2009

PubMed Abstract: Protein import into peroxisomes depends on a complex and dynamic network of protein-protein interactions. Pex14 is a central component of the peroxisomal import machinery and binds the soluble receptors Pex5 and Pex19, which have important function in the assembly of peroxisome matrix and membrane, respectively. We show that the N-terminal domain of Pex14, Pex14(N), adopts a three-helical fold. Pex5 and Pex19 ligand helices bind competitively to the same surface in Pex14(N) albeit with opposite directionality. The molecular recognition involves conserved aromatic side chains in the Pex5 WxxxF/Y motif and a newly identified F/YFxxxF sequence in Pex19. The Pex14-Pex5 complex structure reveals molecular details for a critical interaction in docking Pex5 to the peroxisomal membrane. We show that mutations of Pex14 residues located in the Pex5/Pex19 binding region disrupt Pex5 and/or Pex19 binding in vitro. The corresponding full-length Pex14 variants are impaired in peroxisomal membrane localisation in vivo, showing that the molecular interactions mediated by the N-terminal domain modulate peroxisomal targeting of Pex14.

PubMed: 19197237
DOI: 10.1038/emboj.2009.7

実験手法

SOLUTION NMR