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6ZL0

COPII on membranes, outer coat left-handed rod

Summary for 6ZL0
Entry DOI10.2210/pdb6zl0/pdb
EMDB information11264
DescriptorProtein transport protein SEC31, Protein transport protein SEC13 (2 entities in total)
Functional Keywordsprotein transport, secretion, trafficking
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
More
Total number of polymer chains4
Total formula weight343860.81
Authors
Zanetti, G.,Hutchings, J. (deposition date: 2020-06-30, release date: 2021-02-17, Last modification date: 2024-05-01)
Primary citationHutchings, 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: 33795673
DOI: 10.1038/s41467-021-22110-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (40 Å)
Structure validation

227344

數據於2024-11-13公開中

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