4XZV

Crystal Structure of SLMO1-TRIAP1 Complex

4XZV の概要

• エントリーDOI: 10.2210/pdb4xzv/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose-binding periplasmic protein,TP53-regulated inhibitor of apoptosis 1, Protein slowmo homolog 1, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: apoptosis, lipid transport, mitochondria, complex
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 281086.39

構造登録者

Miliara, X.,Garnett, J.A.,Matthews, S.J. (登録日: 2015-02-05, 公開日: 2016-01-20, 最終更新日: 2024-11-06)

主引用文献

Miliara, X.,Garnett, J.A.,Tatsuta, T.,Abid Ali, F.,Baldie, H.,Perez-Dorado, I.,Simpson, P.,Yague, E.,Langer, T.,Matthews, S.
Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes.
Embo Rep., 16:824-835, 2015

PubMed Abstract: The composition of the mitochondrial membrane is important for its architecture and proper function. Mitochondria depend on a tightly regulated supply of phospholipid via intra-mitochondrial synthesis and by direct import from the endoplasmic reticulum. The Ups1/PRELI-like family together with its mitochondrial chaperones (TRIAP1/Mdm35) represent a unique heterodimeric lipid transfer system that is evolutionary conserved from yeast to man. Work presented here provides new atomic resolution insight into the function of a human member of this system. Crystal structures of free TRIAP1 and the TRIAP1-SLMO1 complex reveal how the PRELI domain is chaperoned during import into the intermembrane mitochondrial space. The structural resemblance of PRELI-like domain of SLMO1 with that of mammalian phoshatidylinositol transfer proteins (PITPs) suggest that they share similar lipid transfer mechanisms, in which access to a buried phospholipid-binding cavity is regulated by conformationally adaptable loops.

PubMed: 26071602
DOI: 10.15252/embr.201540229

実験手法

X-RAY DIFFRACTION (3.58 Å)