6SCT

Cryo-EM structure of the consensus triskelion hub of the clathrin coat complex

「6SBZ」から置き換えられました

6SCT の概要

• エントリーDOI: 10.2210/pdb6sct/pdb
• EMDBエントリー: 0126
• 分子名称: Clathrin heavy chain, Clathrin light chain (2 entities in total)
• 機能のキーワード: clathrin, coat protein, endocytosis, trafficking, transport protein
• 由来する生物種: Sus scrofa (Pig); 詳細
• タンパク質・核酸の鎖数: 15
• 化学式量合計: 1877748.10

構造登録者

Morris, K.L.,Cameron, A.D.,Sessions, R.,Smith, C.J. (登録日: 2019-07-25, 公開日: 2019-10-02, 最終更新日: 2025-07-09)

主引用文献

Morris, K.L.,Jones, J.R.,Halebian, M.,Wu, S.,Baker, M.,Armache, J.P.,Avila Ibarra, A.,Sessions, R.B.,Cameron, A.D.,Cheng, Y.,Smith, C.J.
Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly.
Nat.Struct.Mol.Biol., 26:890-898, 2019

PubMed Abstract: Clathrin forms diverse lattice and cage structures that change size and shape rapidly in response to the needs of eukaryotic cells during clathrin-mediated endocytosis and intracellular trafficking. We present the cryo-EM structure and molecular model of assembled porcine clathrin, providing insights into interactions that stabilize key elements of the clathrin lattice, namely, between adjacent heavy chains, at the light chain-heavy chain interface and within the trimerization domain. Furthermore, we report cryo-EM maps for five different clathrin cage architectures. Fitting structural models to three of these maps shows that their assembly requires only a limited range of triskelion leg conformations, yet inherent flexibility is required to maintain contacts. Analysis of the protein-protein interfaces shows remarkable conservation of contact sites despite architectural variation. These data reveal a universal mode of clathrin assembly that allows variable cage architecture and adaptation of coated vesicle size and shape during clathrin-mediated vesicular trafficking or endocytosis.

PubMed: 31582853
DOI: 10.1038/s41594-019-0292-0

実験手法

ELECTRON MICROSCOPY (4.69 Å)