6mlu
From Proteopedia
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<StructureSection load='6mlu' size='340' side='right' caption='[[6mlu]], [[Resolution|resolution]] 4.00Å' scene=''> | <StructureSection load='6mlu' size='340' side='right' caption='[[6mlu]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6mlu]] is a 2 chain structure. 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 [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> |
| - | </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> | + | </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> |
| + | <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> | ||
</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> | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6mlu" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Drome]] | ||
[[Category: Arlt, H]] | [[Category: Arlt, H]] | ||
[[Category: Farese, V R]] | [[Category: Farese, V R]] | ||
Revision as of 07:21, 31 October 2018
Cryo-EM structure of lipid droplet formation protein Seipin/BSCL2
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