ArticleActa crystallographica. Section F, Structural biology communications2015
Structure of human saposin A at lysosomal pH.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Review
- The proteotranscriptomic characterization of venom in the white seafanOpen biology · 2025Article
- Human Saposin B Ligand Binding and Presentation to α-Galactosidase A.bioRxiv : the preprint server for biology · 2024Article
- A previously unrecognized superfamily of macro-conotoxins includes an inhibitor of the sensory neuron calcium channel Cav2.3.PLoS biology · 2023Article
- A Tetrameric Assembly of Saposin A: Increasing Structural Diversity in Lipid Transfer Proteins.Contact (Thousand Oaks (Ventura County, Calif.)) · 2021Article
- The lipid transfer protein Saposin B does not directly bind CD1d for lipid antigen loading.Wellcome open research · 2019Article
- A Comparative Study of Human Saposins.Molecules (Basel, Switzerland) · 2018Article
- The mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structure.Nature communications · 2018Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The saposins are essential cofactors for the normal lysosomal degradation of complex glycosphingolipids by acid hydrolase enzymes; defects in either saposin or hydrolase function lead to severe metabolic diseases. Saposin A (SapA) activates the enzyme β-galactocerebrosidase (GALC), which catalyzes the breakdown of β-D-galactocerebroside, the principal lipid component of myelin. SapA is known to bind lipids and detergents in a pH-dependent manner; this is accompanied by a striking transition from a `closed' to an `open' conformation. However, previous structures were determined at non-lysosomal pH. This work describes a 1.8 Å resolution X-ray crystal structure determined at the physiologically relevant lysosomal pH 4.8. In the absence of lipid or detergent at pH 4.8, SapA is observeed to adopt a conformation closely resembling the previously determined `closed' conformation, showing that pH alone is not sufficient for the transition to the `open' conformation. Structural alignments reveal small conformational changes, highlighting regions of flexibility.
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