5NXB

Mouse galactocerebrosidase in complex with saposin A

「5N8K」から置き換えられました

5NXB の概要

• エントリーDOI: 10.2210/pdb5nxb/pdb
• 分子名称: Galactocerebrosidase, Prosaposin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: krabbe disease, galactocerebroside, galactosylceramide, galc, sapa, hydrolase
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 171726.63

構造登録者

Graham, S.C.,Hill, C.H.,Deane, J.E. (登録日: 2017-05-09, 公開日: 2017-05-24, 最終更新日: 2024-10-16)

主引用文献

Hill, C.H.,Cook, G.M.,Spratley, S.J.,Fawke, S.,Graham, S.C.,Deane, J.E.
The mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structure.
Nat Commun, 9:151-151, 2018

PubMed Abstract: Sphingolipids are essential components of cellular membranes and defects in their synthesis or degradation cause severe human diseases. The efficient degradation of sphingolipids in the lysosome requires lipid-binding saposin proteins and hydrolytic enzymes. The glycosphingolipid galactocerebroside is the primary lipid component of the myelin sheath and is degraded by the hydrolase β-galactocerebrosidase (GALC). This enzyme requires the saposin SapA for lipid processing and defects in either of these proteins causes a severe neurodegenerative disorder, Krabbe disease. Here we present the structure of a glycosphingolipid-processing complex, revealing how SapA and GALC form a heterotetramer with an open channel connecting the enzyme active site to the SapA hydrophobic cavity. This structure defines how a soluble hydrolase can cleave the polar glycosyl headgroups of these essential lipids from their hydrophobic ceramide tails. Furthermore, the molecular details of this interaction provide an illustration for how specificity of saposin binding to hydrolases is encoded.

PubMed: 29323104
DOI: 10.1038/s41467-017-02361-y

実験手法

X-RAY DIFFRACTION (3.6 Å)