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5A1Y

The structure of the COPI coat linkage IV

Summary for 5A1Y
Entry DOI10.2210/pdb5a1y/pdb
Related5A1U 5A1V 5A1W 5A1X
EMDB information2989
DescriptorADP-RIBOSYLATION FACTOR 1, COATOMER SUBUNIT ALPHA, COATOMER SUBUNIT BETA', ... (8 entities in total)
Functional Keywordstransport protein, copi, coatomer, coated vesicles
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
More
Cellular locationGolgi apparatus: P11076
Cytoplasm . Xenin: Secreted : Q8CIE6
Cytoplasm, cytosol : O55029 Q9QZE5
Cytoplasm : P61924 Q9JIF7 Q5XJY5 O89079
Total number of polymer chains21
Total formula weight1348597.29
Authors
Dodonova, S.O.,Diestelkoetter-Bachert, P.,von Appen, A.,Hagen, W.J.H.,Beck, R.,Beck, M.,Wieland, F.,Briggs, J.A.G. (deposition date: 2015-05-06, release date: 2015-07-08, Last modification date: 2024-05-08)
Primary citationDodonova, S.O.,Diestelkoetter-Bachert, P.,Von Appen, A.,Hagen, W.J.H.,Beck, R.,Beck, M.,Wieland, F.,Briggs, J.A.G.
Vesicular Transport. A Structure of the Copi Coat and the Role of Coat Proteins in Membrane Vesicle Assembly.
Science, 349:195-, 2015
Cited by
PubMed Abstract: Transport of material within cells is mediated by trafficking vesicles that bud from one cellular compartment and fuse with another. Formation of a trafficking vesicle is driven by membrane coats that localize cargo and polymerize into cages to bend the membrane. Although extensive structural information is available for components of these coats, the heterogeneity of trafficking vesicles has prevented an understanding of how complete membrane coats assemble on the membrane. We combined cryo-electron tomography, subtomogram averaging, and cross-linking mass spectrometry to derive a complete model of the assembled coat protein complex I (COPI) coat involved in traffic between the Golgi and the endoplasmic reticulum. The highly interconnected COPI coat structure contradicted the current "adaptor-and-cage" understanding of coated vesicle formation.
PubMed: 26160949
DOI: 10.1126/SCIENCE.AAB1121
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (21 Å)
Structure validation

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