6so5: Difference between revisions

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-====
+==Homo sapiens WRB/CAML heterotetramer in complex with a TRC40 dimer==
-<StructureSection load='6so5' size='340' side='right'caption='[[6so5]]' scene=''>
+<StructureSection load='6so5' size='340' side='right'caption='[[6so5]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
 == 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 [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6so5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SO5 FirstGlance]. <br>
-</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=6so5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6so5 OCA], [https://pdbe.org/6so5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6so5 RCSB], [https://www.ebi.ac.uk/pdbsum/6so5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6so5 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=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6so6|6so6]]</div></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASNA1, ARSA, TRC40 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), WRB, CHD5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CAMLG, CAML ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=6so5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6so5 OCA], [https://pdbe.org/6so5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6so5 RCSB], [https://www.ebi.ac.uk/pdbsum/6so5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6so5 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[https://www.uniprot.org/uniprot/CAMLG_HUMAN CAMLG_HUMAN]] Likely involved in the mobilization of calcium as a result of the TCR/CD3 complex interaction. Binds to cyclophilin B. [[https://www.uniprot.org/uniprot/GET1_HUMAN GET1_HUMAN]] Receptor for GET3/TRC40-mediated insertion of tail-anchored (TA) proteins into the ER membrane.<ref>PMID:21444755</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Membrane protein biogenesis faces the challenge of chaperoning hydrophobic transmembrane helices for faithful membrane insertion. The guided entry of tail-anchored proteins (GET) pathway targets and inserts tail-anchored (TA) proteins into the endoplasmic reticulum (ER) membrane with an insertase (yeast Get1/Get2 or mammalian WRB/CAML) that captures the TA from a cytoplasmic chaperone (Get3 or TRC40, respectively). Here, we present cryo-electron microscopy reconstructions, native mass spectrometry, and structure-based mutagenesis of human WRB/CAML/TRC40 and yeast Get1/Get2/Get3 complexes. Get3 binding to the membrane insertase supports heterotetramer formation, and phosphatidylinositol binding at the heterotetramer interface stabilizes the insertase for efficient TA insertion in vivo. We identify a Get2/CAML cytoplasmic helix that forms a "gating" interaction with Get3/TRC40 important for TA insertion. Structural homology with YidC and the ER membrane protein complex (EMC) implicates an evolutionarily conserved insertion mechanism for divergent substrates utilizing a hydrophilic groove. Thus, we provide a detailed structural and mechanistic framework to understand TA membrane insertion.
+Structural Basis of Tail-Anchored Membrane Protein Biogenesis by the GET Insertase Complex.,McDowell MA, Heimes M, Fiorentino F, Mehmood S, Farkas A, Coy-Vergara J, Wu D, Bolla JR, Schmid V, Heinze R, Wild K, Flemming D, Pfeffer S, Schwappach B, Robinson CV, Sinning I Mol Cell. 2020 Oct 1;80(1):72-86.e7. doi: 10.1016/j.molcel.2020.08.012. Epub 2020, Sep 9. PMID:32910895<ref>PMID:32910895</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6so5" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Large Structures]]
-[[Category: Z-disk]]
+[[Category: Flemming, D]]
+[[Category: Heimes, M]]
+[[Category: McDowell, M A]]
+[[Category: Sinning, I]]
+[[Category: Wild, K]]
+[[Category: Complex]]
+[[Category: Er]]
+[[Category: Insertase]]
+[[Category: Membrane protein]]
+[[Category: Tail-anchor]]