6tqt: Difference between revisions
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==The crystal structure of the MSP domain of human MOSPD2.== | ==The crystal structure of the MSP domain of human MOSPD2.== | ||
<StructureSection load='6tqt' size='340' side='right'caption='[[6tqt]]' scene=''> | <StructureSection load='6tqt' size='340' side='right'caption='[[6tqt]], [[Resolution|resolution]] 1.50Å' 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=6TQT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TQT FirstGlance]. <br> | <table><tr><td colspan='2'>[[6tqt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TQT FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tqt OCA], [http://pdbe.org/6tqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tqt RCSB], [http://www.ebi.ac.uk/pdbsum/6tqt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tqt ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MOSPD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tqt OCA], [http://pdbe.org/6tqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tqt RCSB], [http://www.ebi.ac.uk/pdbsum/6tqt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tqt ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://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 6tqt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Alpy F]] | [[Category: Alpy, F]] | ||
[[Category: Cavarelli J]] | [[Category: Cavarelli, J]] | ||
[[Category: | [[Category: Mattia, T Di]] | ||
[[Category: McEwen | [[Category: McEwen, A G]] | ||
[[Category: Poussin-Courmontagne P]] | [[Category: Poussin-Courmontagne, P]] | ||
[[Category: Tomasetto C]] | [[Category: Tomasetto, C]] | ||
[[Category: Wendling C]] | [[Category: Wendling, C]] | ||
[[Category: Endoplasmic reticulum]] | |||
[[Category: Ffat motif]] | |||
[[Category: Membrane contact site]] | |||
[[Category: Msp domain]] | |||
[[Category: Protein binding]] | |||
