Summary for 6SCT
| Entry DOI | 10.2210/pdb6sct/pdb |
| EMDB information | 0126 |
| Descriptor | Clathrin heavy chain, Clathrin light chain (2 entities in total) |
| Functional Keywords | clathrin, coat protein, endocytosis, trafficking, transport protein |
| Biological source | Sus scrofa (Pig) More |
| Total number of polymer chains | 15 |
| Total formula weight | 1877748.10 |
| Authors | Morris, K.L.,Cameron, A.D.,Sessions, R.,Smith, C.J. (deposition date: 2019-07-25, release date: 2019-10-02, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 31582853DOI: 10.1038/s41594-019-0292-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.69 Å) |
Structure validation
Download full validation report
