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| | <StructureSection load='4uuy' size='340' side='right'caption='[[4uuy]], [[Resolution|resolution]] 2.14Å' scene=''> | | <StructureSection load='4uuy' size='340' side='right'caption='[[4uuy]], [[Resolution|resolution]] 2.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4uuy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UUY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UUY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4uuy]] is a 2 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=4UUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UUY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uuy OCA], [http://pdbe.org/4uuy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uuy RCSB], [http://www.ebi.ac.uk/pdbsum/4uuy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uuy ProSAT]</span></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=4uuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uuy OCA], [https://pdbe.org/4uuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uuy RCSB], [https://www.ebi.ac.uk/pdbsum/4uuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uuy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PEP3_YEAST PEP3_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. 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.<ref>PMID:10978279</ref> <ref>PMID:16601699</ref> | + | [https://www.uniprot.org/uniprot/PEP3_YEAST PEP3_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. 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.<ref>PMID:10978279</ref> <ref>PMID:16601699</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Behrmann, H]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Gohlke, U]] | + | [[Category: Behrmann H]] |
| - | [[Category: Heinemann, U]] | + | [[Category: Gohlke U]] |
| - | [[Category: Endosome]] | + | [[Category: Heinemann U]] |
| - | [[Category: Hop]]
| + | |
| - | [[Category: Membrane fusion]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Vacuole]]
| + | |
| Structural highlights
Function
PEP3_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. 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.[1] [2]
Publication Abstract from PubMed
Membrane fusion at the vacuole, the lysosome equivalent in yeast, requires the HOPS tethering complex, which is recruited by the Rab7 GTPase Ypt7. HOPS provides a template for the assembly of SNAREs and thus likely confers fusion at a distinct position on vacu-oles. Five of the six subunits in HOPS have a similar domain prediction with strong simi-larity to COPII subunits and nuclear porins. Here, we show that Vps18 indeed has a 7-bladed beta-propeller as its N-terminal domain by revealing its structure at 2.14 Angstroem. The Vps18 N-terminal domain can interact with the N-terminal part of Vps11 and also binds to lipids. Although deletion of the Vps18 N-terminal domain does not preclude HOPS assembly, as revealed by negative stain elec-tron microscopy, the complex is instable and cannot support membrane fusion in vitro. We thus conclude that the beta-propeller of Vps18 is required for HOPS stability and function, and that it can serve as a starting point for further structural analyses of the HOPS tethering complex.
Structural identification of the VPS18 beta-propeller reveals a critical role in the hops complex stability and function.,Behrmann H, Lurick A, Kuhlee A, Balderhaar HK, Brocker C, Kummel D, Engelbrecht-Vandre S, Gohlke U, Raunser S, Heinemann U, Ungermann C J Biol Chem. 2014 Oct 16. pii: jbc.M114.602714. PMID:25324549[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Srivastava A, Woolford CA, Jones EW. Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae. Genetics. 2000 Sep;156(1):105-22. PMID:10978279
- ↑ Stroupe C, Collins KM, Fratti RA, Wickner W. Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p. EMBO J. 2006 Apr 19;25(8):1579-89. Epub 2006 Apr 6. PMID:16601699 doi:http://dx.doi.org/7601051
- ↑ Behrmann H, Lurick A, Kuhlee A, Balderhaar HK, Brocker C, Kummel D, Engelbrecht-Vandre S, Gohlke U, Raunser S, Heinemann U, Ungermann C. Structural identification of the VPS18 beta-propeller reveals a critical role in the hops complex stability and function. J Biol Chem. 2014 Oct 16. pii: jbc.M114.602714. PMID:25324549 doi:http://dx.doi.org/10.1074/jbc.M114.602714
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