2Z9A

Crystal Structure of Human Saposin C Dimer in Open Conformation

2Z9A の概要

• エントリーDOI: 10.2210/pdb2z9a/pdb
• 関連するPDBエントリー: 2R0R 2R1Q 2RB3 2qyp
• 分子名称: Proactivator polypeptide, GLYCEROL (3 entities in total)
• 機能のキーワード: lipid binding protein, saposin, activator protein, sap, disease mutation, gaucher disease, glycoprotein, gm2-gangliosidosis, lipid metabolism, lysosome, metachromatic leukodystrophy, sphingolipid metabolism
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Lysosome: P07602
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20483.44

構造登録者

Rossmann, M.,Saenger, W.,Maier, T. (登録日: 2007-09-18, 公開日: 2008-04-29, 最終更新日: 2024-11-20)

主引用文献

Rossmann, M.,Schultz-Heienbrok, R.,Behlke, J.,Remmel, N.,Alings, C.,Sandhoff, K.,Saenger, W.,Maier, T.
Crystal structures of human saposins C and d: implications for lipid recognition and membrane interactions.
Structure, 16:809-817, 2008

PubMed Abstract: Human saposins are essential proteins required for degradation of sphingolipids and lipid antigen presentation. Despite the conserved structural organization of saposins, their distinct modes of interaction with biological membranes are not fully understood. We describe two crystal structures of human saposin C in an "open" configuration with unusual domain swapped homodimers. This form of SapC dimer supports the "clip-on" model for SapC-induced vesicle fusion. In addition, we present the crystal structure of SapD in two crystal forms. They reveal the monomer-monomer interface for the SapD dimer, which was confirmed in solution by analytical ultracentrifugation. The crystal structure of SapD suggests that side chains of Lys10 and Arg17 are involved in initial association with the preferred anionic biological membranes by forming salt bridges with sulfate or phosphate lipid headgroups.

PubMed: 18462685
DOI: 10.1016/j.str.2008.02.016

実験手法

X-RAY DIFFRACTION (2.5 Å)