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5MU7

Crystal Structure of the beta/delta-COPI Core Complex

Summary for 5MU7
Entry DOI10.2210/pdb5mu7/pdb
DescriptorCoatomer subunit beta, Coatomer subunit delta-like protein (3 entities in total)
Functional Keywordscoatomer, copi, beta cop, delta cop, protein transport
Biological sourceChaetomium thermophilum var. thermophilum DSM 1495
More
Cellular locationCytoplasm : G0S6G7
Cytoplasmic vesicle, COPI-coated vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Golgi apparatus membrane ; Peripheral membrane protein ; Cytoplasmic side : G0S6I4
Total number of polymer chains2
Total formula weight62650.29
Authors
Kopp, J.,Aderhold, P.,Wieland, F.,Sinning, I. (deposition date: 2017-01-12, release date: 2017-06-28, Last modification date: 2024-05-08)
Primary citationDodonova, S.O.,Aderhold, P.,Kopp, J.,Ganeva, I.,Rohling, S.,Hagen, W.J.,Sinning, I.,Wieland, F.,Briggs, J.A.
9 angstrom structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments.
Elife, 6:-, 2017
Cited by
PubMed Abstract: COPI coated vesicles mediate trafficking within the Golgi apparatus and between the Golgi and the endoplasmic reticulum. Assembly of a COPI coated vesicle is initiated by the small GTPase Arf1 that recruits the coatomer complex to the membrane, triggering polymerization and budding. The vesicle uncoats before fusion with a target membrane. Coat components are structurally conserved between COPI and clathrin/adaptor proteins. Using cryo-electron tomography and subtomogram averaging, we determined the structure of the COPI coat assembled on membranes in vitro at 9 Å resolution. We also obtained a 2.57 Å resolution crystal structure of βδ-COP. By combining these structures we built a molecular model of the coat. We additionally determined the coat structure in the presence of ArfGAP proteins that regulate coat dissociation. We found that Arf1 occupies contrasting molecular environments within the coat, leading us to hypothesize that some Arf1 molecules may regulate vesicle assembly while others regulate coat disassembly.
PubMed: 28621666
DOI: 10.7554/eLife.26691
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.57 Å)
Structure validation

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