7zty
From Proteopedia
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(New page: '''Unreleased structure''' The entry 7zty is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Vps39 N-terminal domain from Chaetomium thermophilum== | |
| + | <StructureSection load='7zty' size='340' side='right'caption='[[7zty]], [[Resolution|resolution]] 2.89Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7zty]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZTY FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.89Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=7zty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zty OCA], [https://pdbe.org/7zty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zty RCSB], [https://www.ebi.ac.uk/pdbsum/7zty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zty ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/G0RY05_CHATD G0RY05_CHATD] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lysosomes are essential for cellular recycling, nutrient signaling, autophagy, and pathogenic bacteria and viruses invasion. Lysosomal fusion is fundamental to cell survival and requires HOPS, a conserved heterohexameric tethering complex. On the membranes to be fused, HOPS binds small membrane-associated GTPases and assembles SNAREs for fusion, but how the complex fulfills its function remained speculative. Here, we used cryo-electron microscopy to reveal the structure of HOPS. Unlike previously reported, significant flexibility of HOPS is confined to its extremities, where GTPase binding occurs. The SNARE-binding module is firmly attached to the core, therefore, ideally positioned between the membranes to catalyze fusion. Our data suggest a model for how HOPS fulfills its dual functionality of tethering and fusion and indicate why it is an essential part of the membrane fusion machinery. | ||
| - | + | Structure of the HOPS tethering complex, a lysosomal membrane fusion machinery.,Shvarev D, Schoppe J, Konig C, Perz A, Fullbrunn N, Kiontke S, Langemeyer L, Januliene D, Schnelle K, Kummel D, Frohlich F, Moeller A, Ungermann C Elife. 2022 Sep 13;11:e80901. doi: 10.7554/eLife.80901. PMID:36098503<ref>PMID:36098503</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7zty" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chaetomium thermophilum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kiontke S]] | ||
| + | [[Category: Kuemmel D]] | ||
| + | [[Category: Ungermann C]] | ||
Current revision
Structure of Vps39 N-terminal domain from Chaetomium thermophilum
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