5U85

Murine saposin-D (SapD), open conformation

5U85 の概要

• エントリーDOI: 10.2210/pdb5u85/pdb
• 分子名称: Saposin-D (2 entities in total)
• 機能のキーワード: saposin, lipid binding protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18543.36

構造登録者

Gebai, A.,Gorelik, A.,Illes, K.,Nagar, B. (登録日: 2016-12-13, 公開日: 2018-06-13, 最終更新日: 2024-10-23)

主引用文献

Gebai, A.,Gorelik, A.,Nagar, B.
Crystal structure of saposin D in an open conformation.
J. Struct. Biol., 204:145-150, 2018

PubMed Abstract: Saposins are accessory proteins that aid in the degradation of sphingolipids by hydrolytic enzymes. Their structure usually comprises four α-helices arranged in various conformations including an open, V-shaped form that is generally associated with the ability to interact with membranes and/or enzymes to accentuate activity. Saposin D is required by the lysosomal hydrolase, acid ceramidase, which breaks down ceramide into sphingosine and free fatty acid, to display optimal activity. The structure of saposin D was previously determined in an inactive conformation, revealing a monomeric, closed and compact form. Here, we present the crystal structure of the open, V-shaped form of saposin D. The overall shape is similar to the open conformation found in other saposins with slight differences in the angles between the α-helices. The structure forms a dimer that serves to stabilize the hydrophobic surface exposed in the open form, which results in an internal, hydrophobic cavity that could be used to carry extracted membrane lipids.

PubMed: 30026085
DOI: 10.1016/j.jsb.2018.07.011

実験手法

X-RAY DIFFRACTION (1.65 Å)