4DDJ
Crystal structure of saposin A in complex with lauryldimethylamine-N-oxide (LDAO)
Summary for 4DDJ
| Entry DOI | 10.2210/pdb4ddj/pdb |
| Related | 2DOB |
| Descriptor | Saposin-A, LAURYL DIMETHYLAMINE-N-OXIDE (3 entities in total) |
| Functional Keywords | saposin fold, sphingolipid activator protein, galactosylceramide, lauryldimethylamine-n-oxide, lipid, detergent, lysosome, lipid binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 13649.53 |
| Authors | Popovic, K.,Prive, G.G. (deposition date: 2012-01-18, release date: 2012-02-15, Last modification date: 2024-11-20) |
| Primary citation | Popovic, K.,Holyoake, J.,Pomes, R.,Prive, G.G. Structure of saposin A lipoprotein discs. Proc.Natl.Acad.Sci.USA, 109:2908-2912, 2012 Cited by PubMed Abstract: The saposins are small, membrane-active proteins that exist in both soluble and lipid-bound states. Saposin A has roles in sphingolipid catabolism and transport and is required for the breakdown of galactosylceramide by β-galactosylceramidase. In the absence of lipid, saposin A adopts a closed monomeric apo conformation typical of this family. To study a lipid-bound state of this protein, we determined the crystal structure of saposin A in the presence of detergent to 1.9 Å resolution. The structure reveals two chains of saposin A in an open conformation encapsulating 40 internally bound detergent molecules organized in a highly ordered bilayer-like hydrophobic core. The complex provides a high-resolution view of a discoidal lipoprotein particle in which all of the internalized acyl chains are resolved. Saposin A lipoprotein discs exhibit limited selectivity with respect to the incorporated lipid, and can solubilize phospholipids, sphingolipids, and cholesterol into discrete, monodisperse particles with mass of approximately 27 kDa. These discs may be the smallest possible lipoprotein structures that are stabilized by lipid self-assembly. PubMed: 22308394DOI: 10.1073/pnas.1115743109 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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