6mhm
From Proteopedia
(Difference between revisions)
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<StructureSection load='6mhm' size='340' side='right'caption='[[6mhm]], [[Resolution|resolution]] 2.74Å' scene=''> | <StructureSection load='6mhm' size='340' side='right'caption='[[6mhm]], [[Resolution|resolution]] 2.74Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6mhm]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6mhm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MHM FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.743Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JRY:hexylcarbamic+acid'>JRY</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | < | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6mhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mhm OCA], [https://pdbe.org/6mhm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mhm RCSB], [https://www.ebi.ac.uk/pdbsum/6mhm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mhm ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ASAH1_HUMAN ASAH1_HUMAN] Farber disease;Spinal muscular atrophy-progressive myoclonic epilepsy syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. |
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ASAH1_HUMAN ASAH1_HUMAN] Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (PubMed:10610716, PubMed:7744740, PubMed:15655246, PubMed:11451951). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (PubMed:10610716). Has a higher catalytic efficiency towards C12-ceramides versus other ceramides (PubMed:7744740, PubMed:15655246). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (PubMed:12764132, PubMed:12815059). For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro-dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used (PubMed:12764132). Has also an N-acylethanolamine hydrolase activity (PubMed:15655246). By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes (PubMed:17713573). Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis (By similarity). By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis (PubMed:22261821).[UniProtKB:Q9WV54]<ref>PMID:10610716</ref> <ref>PMID:11451951</ref> <ref>PMID:12764132</ref> <ref>PMID:12815059</ref> <ref>PMID:15655246</ref> <ref>PMID:17713573</ref> <ref>PMID:22261821</ref> <ref>PMID:7744740</ref> <ref>PMID:10610716</ref> Isoform 2: May directly regulate steroidogenesis by binding the nuclear receptor NR5A1 and negatively regulating its transcriptional activity.<ref>PMID:22927646</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6mhm" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6mhm" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Ceramidase 3D PDB structures|Ceramidase 3D PDB structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Dementiev | + | [[Category: Dementiev A]] |
| - | [[Category: Doan | + | [[Category: Doan N]] |
| - | [[Category: Joachimiak | + | [[Category: Joachimiak A]] |
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Revision as of 06:32, 11 October 2023
Crystal structure of human acid ceramidase in covalent complex with carmofur
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