6mlu

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<SX load='6mlu' size='340' side='right' viewer='molstar' caption='[[6mlu]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
<SX load='6mlu' size='340' side='right' viewer='molstar' caption='[[6mlu]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
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<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>
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<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 ==
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[[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>
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[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>
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<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&reg;/PubMed&reg;, 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__
</SX>
</SX>
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[[Category: Drome]]
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[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arlt, H]]
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[[Category: Arlt H]]
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[[Category: Farese, V R]]
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[[Category: Farese VR]]
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[[Category: Liao, M]]
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[[Category: Liao M]]
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[[Category: Sui, X]]
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[[Category: Sui X]]
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[[Category: Walther, C T]]
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[[Category: Walther CT]]
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[[Category: Lipid droplet formation]]
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[[Category: Lipid storage]]
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[[Category: Lipodystrophy]]
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[[Category: Membrane protein]]
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Current revision

Cryo-EM structure of lipid droplet formation protein Seipin/BSCL2

6mlu, resolution 4.00Å

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