6ZGA
COPII on membranes, inner coat
Summary for 6ZGA
| Entry DOI | 10.2210/pdb6zga/pdb |
| EMDB information | 11199 |
| Descriptor | Protein transport protein SEC23, Protein transport protein SEC24, Small COPII coat GTPase SAR1, ... (8 entities in total) |
| Functional Keywords | protein transport, secretion, trafficking |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 8 |
| Total formula weight | 422935.92 |
| Authors | Zanetti, G.,Hutchings, J.,Cheung, A.C.M. (deposition date: 2020-06-18, release date: 2021-02-17, Last modification date: 2021-04-14) |
| Primary citation | Hutchings, J.,Stancheva, V.G.,Brown, N.R.,Cheung, A.C.M.,Miller, E.A.,Zanetti, G. Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network. Nat Commun, 12:2034-2034, 2021 Cited by PubMed Abstract: COPII mediates Endoplasmic Reticulum to Golgi trafficking of thousands of cargoes. Five essential proteins assemble into a two-layer architecture, with the inner layer thought to regulate coat assembly and cargo recruitment, and the outer coat forming cages assumed to scaffold membrane curvature. Here we visualise the complete, membrane-assembled COPII coat by cryo-electron tomography and subtomogram averaging, revealing the full network of interactions within and between coat layers. We demonstrate the physiological importance of these interactions using genetic and biochemical approaches. Mutagenesis reveals that the inner coat alone can provide membrane remodelling function, with organisational input from the outer coat. These functional roles for the inner and outer coats significantly move away from the current paradigm, which posits membrane curvature derives primarily from the outer coat. We suggest these interactions collectively contribute to coat organisation and membrane curvature, providing a structural framework to understand regulatory mechanisms of COPII trafficking and secretion. PubMed: 33795673DOI: 10.1038/s41467-021-22110-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.6 Å) |
Structure validation
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