5U85
Murine saposin-D (SapD), open conformation
Summary for 5U85
| Entry DOI | 10.2210/pdb5u85/pdb |
| Descriptor | Saposin-D (2 entities in total) |
| Functional Keywords | saposin, lipid binding protein |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 18543.36 |
| Authors | Gebai, A.,Gorelik, A.,Illes, K.,Nagar, B. (deposition date: 2016-12-13, release date: 2018-06-13, Last modification date: 2024-10-23) |
| Primary citation | Gebai, A.,Gorelik, A.,Nagar, B. Crystal structure of saposin D in an open conformation. J. Struct. Biol., 204:145-150, 2018 Cited by 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: 30026085DOI: 10.1016/j.jsb.2018.07.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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