EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Structure of the membrane-assembled retromer coat determined by cryo-electron tomography.
ジャーナル・号・ページ	Nature, Vol. 561, Issue 7724, Page 561-564, Year 2018
掲載日	2018年9月17日
著者	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 要旨	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.
リンク	Nature / PubMed:30224749 / PubMed Central
手法	EM (サブトモグラム平均) / EM (トモグラフィー) / X線回折
解像度	1.52 - 37.0 Å
構造データ	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. 手法: EM (サブトモグラム平均) / 解像度: 11.4 Å EMDB-0155: Retromer-Vps5: low-resolution overview map centred on the Vps35/29 arch. 手法: EM (サブトモグラム平均) / 解像度: 11.8 Å EMDB-0156: Retromer-Vps5: map centred on the Vps35/29 arch. 手法: EM (サブトモグラム平均) / 解像度: 8.7 Å EMDB-0157: Retromer-Vps5: map centred on the leg of the Vps35/29 arch. 手法: EM (サブトモグラム平均) / 解像度: 9.1 Å EMDB-0158: Retromer-Vps5: map centred on the Vps5 layer under the Vps35/29 arch. 手法: EM (サブトモグラム平均) / 解像度: 9.4 Å EMDB-0159: Retromer-Vps5: map centred on the Vps5 layer under the Vps26 dimer. 手法: EM (サブトモグラム平均) / 解像度: 8.9 Å EMDB-0160: Retromer-Vps5: map centred on the Vps26 dimer. 手法: EM (サブトモグラム平均) / 解像度: 8.9 Å EMDB-0161: Retromer arch structures in the cell. 手法: EM (サブトモグラム平均) / 解像度: 37.0 Å EMDB-0162: Retromer-Vps5: membrane tubules, tomogram 7. 手法: EM (トモグラフィー) EMDB-0163: Retromer-Vps5: membrane tubules, tomogram 70. 手法: EM (トモグラフィー) PDB-5w8m: Crystal structure of Chaetomium thermophilum Vps29 手法: X-RAY DIFFRACTION / 解像度: 1.52 Å
化合物	ChemComp-PGE: TRIETHYLENE GLYCOL / トリエチレングリコ-ル ChemComp-GOL: GLYCEROL / グリセロ-ル ChemComp-HOH: WATER
由来	Chaetomium thermophilum var. thermophilum DSM 1495 (菌類) chaetomium thermophilum (strain dsm 1495 / cbs 144.50 / imi 039719) (菌類) chaetomium thermophilum (菌類) Chlamydomonas reinhardtii (クラミドモナス)
キーワード	ENDOCYTOSIS / endosome / retromer / vps29 / PROTEIN TRANSPORT / sorting nexin / BAR / membrane trafficking