7zu0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:42, 24 July 2024) (edit) (undo)
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7zu0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZU0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7zu0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZU0 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=7zu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zu0 OCA], [https://pdbe.org/7zu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zu0 RCSB], [https://www.ebi.ac.uk/pdbsum/7zu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zu0 ProSAT]</span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.4&#8491;</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=7zu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zu0 OCA], [https://pdbe.org/7zu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zu0 RCSB], [https://www.ebi.ac.uk/pdbsum/7zu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zu0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/PEP5_YEAST PEP5_YEAST]] Required for vacuolar biogenesis and for trafficking of hydrolase precursors to the vacuole. Mediates transport at the vacuolar membrane where it may be responsible for tethering transport vesicles on the target membranes. It is required for gluconeogenic growth of yeast. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion (PubMed:3062374, PubMed:10978279, PubMed:10944212, PubMed:16601699). Acts as component of the CORVET complex that is required for transport between endosome and vacuole. CORVET is an effector for the endosomal Rab GTPase VPS21 (PubMed:17488625). Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation (PubMed:22570702).<ref>PMID:10944212</ref> <ref>PMID:10978279</ref> <ref>PMID:16601699</ref> <ref>PMID:17488625</ref> <ref>PMID:22570702</ref> <ref>PMID:3062374</ref>
+
[https://www.uniprot.org/uniprot/VAM6_YEAST VAM6_YEAST] Required for vacuolar assembly. Acts as a component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.<ref>PMID:16601699</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== 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.
+
Cells depend on their endolysosomal system for nutrient uptake and downregulation of plasma membrane proteins. These processes rely on endosomal maturation, which requires multiple membrane fusion steps. Early endosome fusion is promoted by the Rab5 GTPase and its effector, the hexameric CORVET tethering complex, which is homologous to the lysosomal HOPS. How these related complexes recognize their specific target membranes remains entirely elusive. Here, we solve the structure of CORVET by cryo-electron microscopy and revealed its minimal requirements for membrane tethering. As expected, the core of CORVET and HOPS resembles each other. However, the function-defining subunits show marked structural differences. Notably, we discover that unlike HOPS, CORVET depends not only on Rab5 but also on phosphatidylinositol-3-phosphate (PI3P) and membrane lipid packing defects for tethering, implying that an organelle-specific membrane code enables fusion. Our data suggest that both shape and membrane interactions of CORVET and HOPS are conserved in metazoans, thus providing a paradigm how tethering complexes function.
-
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. pii: 80901. doi: 10.7554/eLife.80901. PMID:36098503<ref>PMID:36098503</ref>
+
Structure of the endosomal CORVET tethering complex.,Shvarev D, Konig C, Susan N, Langemeyer L, Walter S, Perz A, Frohlich F, Ungermann C, Moeller A Nat Commun. 2024 Jun 19;15(1):5227. doi: 10.1038/s41467-024-49137-9. PMID:38898033<ref>PMID:38898033</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 7zu0" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 7zu0" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
 +
*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
== References ==
== References ==
<references/>
<references/>

Current revision

HOPS tethering complex from yeast

PDB ID 7zu0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7zu0"
Personal tools