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	Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 26, Issue 10, Page 890-898, Year 2019
Publish date	Oct 3, 2019
Authors	Kyle L Morris / Joseph R Jones / Mary Halebian / Shenping Wu / Michael Baker / Jean-Paul Armache / Amaurys Avila Ibarra / Richard B Sessions / Alexander D Cameron / Yifan Cheng / Corinne J Smith /
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. ...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.
External links	Nat Struct Mol Biol / PubMed:31582853 / PubMed Central
Methods	EM (single particle)
Resolution	4.69 - 23.68 Å
Structure data	EMDB-0114: Cryo-EM structure of the 28 triskelia mini clathrin coat complex Method: EM (single particle) / Resolution: 9.07 Å EMDB-0115: Cryo-EM structure of the 32 triskelia sweet potato clathrin coat complex Method: EM (single particle) / Resolution: 23.68 Å EMDB-0116: Cryo-EM structure of the 36 triskelia D6 barrel clathrin coat complex Method: EM (single particle) / Resolution: 12.18 Å EMDB-0118: Cryo-EM structure of the 36 triskelia tennis ball clathrin coat complex Method: EM (single particle) / Resolution: 13.75 Å EMDB-0120: Cryo-EM structure of the 37 triskelia big apple clathrin coat complex Method: EM (single particle) / Resolution: 23.68 Å EMDB-0121: Cryo-EM structure of the hub of the 28 triskelia mini clathrin coat complex Method: EM (single particle) / Resolution: 5.08 Å EMDB-0122: Cryo-EM structure of the hub of the 32 triskelia sweet potato clathrin coat complex Method: EM (single particle) / Resolution: 7.79 Å EMDB-0123: Cryo-EM structure of the hub of the 36 triskelia D6 barrel clathrin coat complex Method: EM (single particle) / Resolution: 7.66 Å EMDB-0124: Cryo-EM structure of the hub of the 36 triskelia tennis ball clathrin coat complex Method: EM (single particle) / Resolution: 6.93 Å EMDB-0125: Cryo-EM structure of the hub of the 37 triskelia big apple clathrin coat complex Method: EM (single particle) / Resolution: 7.53 Å 0126 6sct EMDB-0126: Cryo-EM structure of the consensus hub of the clathrin coat complex PDB-6sct: Cryo-EM structure of the consensus triskelion hub of the clathrin coat complex Method: EM (single particle) / Resolution: 4.69 Å
Source	sus scrofa (pig) Pig (pig)
Keywords	TRANSPORT PROTEIN / clathrin / coat protein / endocytosis / trafficking