3MK4

X-Ray structure of human PEX3 in complex with a PEX19 derived peptide

3MK4 の概要

• エントリーDOI: 10.2210/pdb3mk4/pdb
• 分子名称: Peroxisomal biogenesis factor 3, Peroxisomal biogenesis factor 19 (3 entities in total)
• 機能のキーワード: membrane, peroxisome, protein transport
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Peroxisome membrane; Multi-pass membrane protein: P56589; Cytoplasm: P40855
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39824.37

構造登録者

Schmidt, F.,Treiber, N.,Dodt, G.,Stehle, T. (登録日: 2010-04-14, 公開日: 2010-06-30, 最終更新日: 2024-04-03)

主引用文献

Schmidt, F.,Treiber, N.,Zocher, G.,Bjelic, S.,Steinmetz, M.O.,Kalbacher, H.,Stehle, T.,Dodt, G.
Insights into peroxisome function from the structure of PEX3 in complex with a soluble fragment of PEX19
J.Biol.Chem., 285:25410-25417, 2010

PubMed Abstract: The human peroxins PEX3 and PEX19 play a central role in peroxisomal membrane biogenesis. The membrane-anchored PEX3 serves as the receptor for cytosolic PEX19, which in turn recognizes newly synthesized peroxisomal membrane proteins. After delivering these proteins to the peroxisomal membrane, PEX19 is recycled to the cytosol. The molecular mechanisms underlying these processes are not well understood. Here, we report the crystal structure of the cytosolic domain of PEX3 in complex with a PEX19-derived peptide. PEX3 adopts a novel fold that is best described as a large helical bundle. A hydrophobic groove at the membrane-distal end of PEX3 engages the PEX19 peptide with nanomolar affinity. Mutagenesis experiments identify phenylalanine 29 in PEX19 as critical for this interaction. Because key PEX3 residues involved in complex formation are highly conserved across species, the observed binding mechanism is of general biological relevance.

PubMed: 20554521
DOI: 10.1074/jbc.M110.138503

実験手法

X-RAY DIFFRACTION (2.42 Å)