Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure of the membrane-assembled retromer coat determined by cryo-electron tomography.
Journal, issue, pages	Nature, Vol. 561, Issue 7724, Page 561-564, Year 2018
Publish date	Sep 17, 2018
Authors	Oleksiy Kovtun / Natalya Leneva / Yury S Bykov / Nicholas Ariotti / Rohan D Teasdale / Miroslava Schaffer / Benjamin D Engel / David J Owen / John A G Briggs / Brett M Collins /
PubMed Abstract	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 ...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. Conserved in eukaryotes, retromer controls the cellular localization and homeostasis of hundreds of transmembrane proteins, and its disruption is associated with major neurodegenerative disorders. 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.
External links	Nature / PubMed:30224749 / PubMed Central
Methods	EM (subtomogram averaging) / EM (tomography) / X-ray diffraction
Resolution	1.52 - 37.0 Å
Structure data	0154 6h7w EMDB-0154: Retromer-Vps5: low-resolution overview map centred on the Vps26 dimer. PDB-6h7w: Model of retromer-Vps5 complex assembled on membrane. Method: EM (subtomogram averaging) / Resolution: 11.4 Å EMDB-0155: Retromer-Vps5: low-resolution overview map centred on the Vps35/29 arch. Method: EM (subtomogram averaging) / Resolution: 11.8 Å EMDB-0156: Retromer-Vps5: map centred on the Vps35/29 arch. Method: EM (subtomogram averaging) / Resolution: 8.7 Å EMDB-0157: Retromer-Vps5: map centred on the leg of the Vps35/29 arch. Method: EM (subtomogram averaging) / Resolution: 9.1 Å EMDB-0158: Retromer-Vps5: map centred on the Vps5 layer under the Vps35/29 arch. Method: EM (subtomogram averaging) / Resolution: 9.4 Å EMDB-0159: Retromer-Vps5: map centred on the Vps5 layer under the Vps26 dimer. Method: EM (subtomogram averaging) / Resolution: 8.9 Å EMDB-0160: Retromer-Vps5: map centred on the Vps26 dimer. Method: EM (subtomogram averaging) / Resolution: 8.9 Å EMDB-0161: Retromer arch structures in the cell. Method: EM (subtomogram averaging) / Resolution: 37.0 Å EMDB-0162: Retromer-Vps5: membrane tubules, tomogram 7. Method: EM (tomography) EMDB-0163: Retromer-Vps5: membrane tubules, tomogram 70. Method: EM (tomography) PDB-5w8m: Crystal structure of Chaetomium thermophilum Vps29 Method: X-RAY DIFFRACTION / Resolution: 1.52 Å
Chemicals	ChemComp-PGE: TRIETHYLENE GLYCOL / Polyethylene glycol ChemComp-GOL: GLYCEROL / Glycerol ChemComp-HOH: WATER / Water
Source	Chaetomium thermophilum var. thermophilum DSM 1495 (fungus) chaetomium thermophilum (strain dsm 1495 / cbs 144.50 / imi 039719) (fungus) chaetomium thermophilum (fungus) Chlamydomonas reinhardtii (plant)
Keywords	ENDOCYTOSIS / endosome / retromer / vps29 / PROTEIN TRANSPORT / sorting nexin / BAR / membrane trafficking