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| | <StructureSection load='5w8m' size='340' side='right'caption='[[5w8m]], [[Resolution|resolution]] 1.52Å' scene=''> | | <StructureSection load='5w8m' size='340' side='right'caption='[[5w8m]], [[Resolution|resolution]] 1.52Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5w8m]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_144.50 Cbs 144.50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W8M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W8M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5w8m]] is a 6 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=5W8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W8M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.52Å</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=5w8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w8m OCA], [http://pdbe.org/5w8m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w8m RCSB], [http://www.ebi.ac.uk/pdbsum/5w8m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w8m ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=5w8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w8m OCA], [https://pdbe.org/5w8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w8m RCSB], [https://www.ebi.ac.uk/pdbsum/5w8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w8m ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0RZB5_CHATD G0RZB5_CHATD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Vacuolar protein sorting-associated protein|Vacuolar protein sorting-associated protein]] | + | *[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cbs 144 50]] | + | [[Category: Chaetomium thermophilum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Collins, B M]] | + | [[Category: Collins BM]] |
| - | [[Category: Leneva, N]] | + | [[Category: Leneva N]] |
| - | [[Category: Endocytosis]]
| + | |
| - | [[Category: Endosome]]
| + | |
| - | [[Category: Retromer]]
| + | |
| - | [[Category: Vps29]]
| + | |
| Structural highlights
Function
G0RZB5_CHATD
Publication Abstract from PubMed
Eukaryotic cells traffic proteins and lipids between different compartments using protein-coated vesicles and tubules. The retromer complex is required to generate cargo-selective tubulovesicular carriers from endosomal membranes(1-3). Conserved in eukaryotes, retromer controls the cellular localization and homeostasis of hundreds of transmembrane proteins, and its disruption is associated with major neurodegenerative disorders(4-7). How retromer is assembled and how it is recruited to form coated tubules is not known. Here we describe the structure of the retromer complex (Vps26-Vps29-Vps35) assembled on membrane tubules with the bin/amphiphysin/rvs-domain-containing sorting nexin protein Vps5, using cryo-electron tomography and subtomogram averaging. This reveals a membrane-associated Vps5 array, from which arches of retromer extend away from the membrane surface. Vps35 forms the 'legs' of these arches, and Vps29 resides at the apex where it is free to interact with regulatory factors. The bases of the arches connect to each other and to Vps5 through Vps26, and the presence of the same arches on coated tubules within cells confirms their functional importance. Vps5 binds to Vps26 at a position analogous to the previously described cargo- and Snx3-binding site, which suggests the existence of distinct retromer-sorting nexin assemblies. The structure provides insight into the architecture of the coat and its mechanism of assembly, and suggests that retromer promotes tubule formation by directing the distribution of sorting nexin proteins on the membrane surface while providing a scaffold for regulatory-protein interactions.
Structure of the membrane-assembled retromer coat determined by cryo-electron tomography.,Kovtun O, Leneva N, Bykov YS, Ariotti N, Teasdale RD, Schaffer M, Engel BD, Owen DJ, Briggs JAG, Collins BM Nature. 2018 Sep 17. pii: 10.1038/s41586-018-0526-z. doi:, 10.1038/s41586-018-0526-z. PMID:30224749[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kovtun O, Leneva N, Bykov YS, Ariotti N, Teasdale RD, Schaffer M, Engel BD, Owen DJ, Briggs JAG, Collins BM. Structure of the membrane-assembled retromer coat determined by cryo-electron tomography. Nature. 2018 Sep 17. pii: 10.1038/s41586-018-0526-z. doi:, 10.1038/s41586-018-0526-z. PMID:30224749 doi:http://dx.doi.org/10.1038/s41586-018-0526-z
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