5u85
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='5u85' size='340' side='right' caption='[[5u85]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='5u85' size='340' side='right' caption='[[5u85]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5u85]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U85 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5u85]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U85 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U85 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5u85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u85 OCA], [http://pdbe.org/5u85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u85 RCSB], [http://www.ebi.ac.uk/pdbsum/5u85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u85 ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Psap, Sgp1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5u85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u85 OCA], [http://pdbe.org/5u85 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u85 RCSB], [http://www.ebi.ac.uk/pdbsum/5u85 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u85 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/SAP_MOUSE SAP_MOUSE]] Prosaposin: Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling.<ref>PMID:23690594</ref> Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate.[UniProtKB:P07602] Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases.[UniProtKB:P07602] Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).[UniProtKB:P07602] Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.[UniProtKB:P07602] | [[http://www.uniprot.org/uniprot/SAP_MOUSE SAP_MOUSE]] Prosaposin: Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling.<ref>PMID:23690594</ref> Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate.[UniProtKB:P07602] Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases.[UniProtKB:P07602] Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).[UniProtKB:P07602] Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.[UniProtKB:P07602] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Saposins are accessory proteins that aid in the degradation of sphingolipids by hydrolytic enzymes. Their structure usually comprises four alpha-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 alpha-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. | ||
| + | |||
| + | Crystal structure of saposin D in an open conformation.,Gebai A, Gorelik A, Nagar B J Struct Biol. 2018 Jul 17. pii: S1047-8477(18)30169-2. doi:, 10.1016/j.jsb.2018.07.011. PMID:30026085<ref>PMID:30026085</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5u85" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Lk3 transgenic mice]] | ||
[[Category: Gebai, A]] | [[Category: Gebai, A]] | ||
[[Category: Gorelik, A]] | [[Category: Gorelik, A]] | ||
Revision as of 19:01, 1 August 2018
Murine saposin-D (SapD), open conformation
| |||||||||||
Categories: Lk3 transgenic mice | Gebai, A | Gorelik, A | Illes, K | Nagar, B | Hydrolase | Saposin
