6tqs
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==The crystal structure of the MSP domain of human MOSPD2 in complex with the conventional FFAT motif of ORP1.== |
| - | <StructureSection load='6tqs' size='340' side='right'caption='[[6tqs]]' scene=''> | + | <StructureSection load='6tqs' size='340' side='right'caption='[[6tqs]], [[Resolution|resolution]] 2.25Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6tqs]] is a 11 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=6TQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TQS FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TFA:TRIFLUOROACETIC+ACID'>TFA</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=6tqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tqs OCA], [https://pdbe.org/6tqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tqs RCSB], [https://www.ebi.ac.uk/pdbsum/6tqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tqs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MSPD2_HUMAN MSPD2_HUMAN] Endoplasmic reticulum-anchored receptor which modulates interorganelle contacts by interacting with other organelle-bound proteins via their FFAT motif (PubMed:29858488). Might have a more important role in endoplasmic reticulum and endosomes contacts (PubMed:29858488). Promotes migration of primary monocytes and neutrophils, in response to various chemokines (PubMed:28137892).<ref>PMID:28137892</ref> <ref>PMID:29858488</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Organelles are physically connected in membrane contact sites. The endoplasmic reticulum possesses three major receptors, VAP-A, VAP-B, and MOSPD2, which interact with proteins at the surface of other organelles to build contacts. VAP-A, VAP-B, and MOSPD2 contain an MSP domain, which binds a motif named FFAT (two phenylalanines in an acidic tract). In this study, we identified a non-conventional FFAT motif where a conserved acidic residue is replaced by a serine/threonine. We show that phosphorylation of this serine/threonine is critical for non-conventional FFAT motifs (named Phospho-FFAT) to be recognized by the MSP domain. Moreover, structural analyses of the MSP domain alone or in complex with conventional and Phospho-FFAT peptides revealed new mechanisms of interaction. Based on these new insights, we produced a novel prediction algorithm, which expands the repertoire of candidate proteins with a Phospho-FFAT that are able to create membrane contact sites. Using a prototypical tethering complex made by STARD3 and VAP, we showed that phosphorylation is instrumental for the formation of ER-endosome contacts, and their sterol transfer function. This study reveals that phosphorylation acts as a general switch for inter-organelle contacts. | ||
| + | |||
| + | FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts.,Di Mattia T, Martinet A, Ikhlef S, McEwen AG, Nomine Y, Wendling C, Poussin-Courmontagne P, Voilquin L, Eberling P, Ruffenach F, Cavarelli J, Slee J, Levine TP, Drin G, Tomasetto C, Alpy F EMBO J. 2020 Oct 30:e104369. doi: 10.15252/embj.2019104369. PMID:33124732<ref>PMID:33124732</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6tqs" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Alpy F]] |
| + | [[Category: Cavarelli J]] | ||
| + | [[Category: Di Mattia T]] | ||
| + | [[Category: McEwen AG]] | ||
| + | [[Category: Poussin-Courmontagne P]] | ||
| + | [[Category: Tomasetto C]] | ||
| + | [[Category: Wendling C]] | ||
Current revision
The crystal structure of the MSP domain of human MOSPD2 in complex with the conventional FFAT motif of ORP1.
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