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| | ==Cryo-EM structure of lipid droplet formation protein Seipin/BSCL2== | | ==Cryo-EM structure of lipid droplet formation protein Seipin/BSCL2== |
| - | <StructureSection load='6mlu' size='340' side='right' caption='[[6mlu]], [[Resolution|resolution]] 4.00Å' scene=''> | + | <SX load='6mlu' size='340' side='right' viewer='molstar' caption='[[6mlu]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mlu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MLU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MLU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mlu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MLU FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Seipin, CG9904 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</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=6mlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mlu OCA], [http://pdbe.org/6mlu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mlu RCSB], [http://www.ebi.ac.uk/pdbsum/6mlu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mlu ProSAT]</span></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=6mlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mlu OCA], [https://pdbe.org/6mlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mlu RCSB], [https://www.ebi.ac.uk/pdbsum/6mlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mlu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BSCL2_DROME BSCL2_DROME]] Is a regulator of lipid catabolism essential for adipocyte differentiation. May also be involved in the central regulation of energy homeostasis (By similarity). Necessary for correct lipid storage and lipid droplets maintenance; plays a tissue-autonomous role in controlling lipid storage in adipocytes and in preventing ectopic lipid droplet formation in non-adipose tissues. May participate in phosphatidic acid metabolism and subsequently down-regulate lipogenesis.[UniProtKB:Q9Z2E9]<ref>PMID:21533227</ref> | + | [https://www.uniprot.org/uniprot/BSCL2_DROME BSCL2_DROME] Is a regulator of lipid catabolism essential for adipocyte differentiation. May also be involved in the central regulation of energy homeostasis (By similarity). Necessary for correct lipid storage and lipid droplets maintenance; plays a tissue-autonomous role in controlling lipid storage in adipocytes and in preventing ectopic lipid droplet formation in non-adipose tissues. May participate in phosphatidic acid metabolism and subsequently down-regulate lipogenesis.[UniProtKB:Q9Z2E9]<ref>PMID:21533227</ref> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Metabolic energy is stored in cells primarily as triacylglycerols in lipid droplets (LDs), and LD dysregulation leads to metabolic diseases. The formation of monolayer-bound LDs from the endoplasmic reticulum (ER) bilayer is poorly understood, but the ER protein seipin is essential to this process. In this study, we report a cryo-electron microscopy structure and functional characterization of Drosophila melanogaster seipin. The structure reveals a ring-shaped dodecamer with the luminal domain of each monomer resolved at approximately 4.0 A. Each luminal domain monomer exhibits two distinctive features: a hydrophobic helix (HH) positioned toward the ER bilayer and a beta-sandwich domain with structural similarity to lipid-binding proteins. This structure and our functional testing in cells suggest a model in which seipin oligomers initially detect forming LDs in the ER via HHs and subsequently act as membrane anchors to enable lipid transfer and LD growth.
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| - | Cryo-electron microscopy structure of the lipid droplet-formation protein seipin.,Sui X, Arlt H, Brock KP, Lai ZW, DiMaio F, Marks DS, Liao M, Farese RV Jr, Walther TC J Cell Biol. 2018 Oct 16. pii: jcb.201809067. doi: 10.1083/jcb.201809067. PMID:30327422<ref>PMID:30327422</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 6mlu" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Arlt, H]] | + | [[Category: Large Structures]] |
| - | [[Category: Farese, V R]] | + | [[Category: Arlt H]] |
| - | [[Category: Liao, M]] | + | [[Category: Farese VR]] |
| - | [[Category: Sui, X]] | + | [[Category: Liao M]] |
| - | [[Category: Walther, C T]] | + | [[Category: Sui X]] |
| - | [[Category: Lipid droplet formation]]
| + | [[Category: Walther CT]] |
| - | [[Category: Lipid storage]]
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| - | [[Category: Lipodystrophy]]
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| - | [[Category: Membrane protein]]
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