1R4X

Crystal Structure Analys of the Gamma-COPI Appendage domain

Summary for 1R4X

• Entry DOI: 10.2210/pdb1r4x/pdb
• Related: 1B9K 1E42 1PZD
• Descriptor: Coatomer gamma subunit, MAGNESIUM ION (3 entities in total)
• Functional Keywords: appendage; beta sandwich; coatomer; adp-ribosylation factors, protein transport
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q9Y678
• Total number of polymer chains: 1
• Total formula weight: 31249.43

Authors

Watson, P.J.,Frigerio, G.,Collins, B.M.,Duden, R.,Owen, D.J. (deposition date: 2003-10-09, release date: 2003-10-28, Last modification date: 2024-11-13)

Primary citation

Watson, P.J.,Frigerio, G.,Collins, B.M.,Duden, R.,Owen, D.J.
Gamma-COP appendage domain - structure and function
Traffic, 5:79-88, 2004

PubMed Abstract: COPI-coated vesicles mediate retrograde transport from the Golgi back to the ER and intra-Golgi transport. The cytosolic precursor of the COPI coat, the heptameric coatomer complex, can be thought of as composed of two subcomplexes. The first consists of the beta-, gamma-, delta- and zeta-COP subunits which are distantly homologous to AP clathrin adaptor subunits. The second consists of the alpha-, beta'- and epsilon-COP subunits. Here, we present the structure of the appendage domain of gamma-COP and show that it has a similar overall fold as the alpha-appendage of AP2. Again, like the alpha-appendage the gamma-COP appendage possesses a single protein/protein interaction site on its platform subdomain. We show that in yeast this site binds to the ARFGAP Glo3p, and in mammalian gamma-COP this site binds to a Glo3p orthologue, ARFGAP2. On the basis of mutations in the yeast homologue of gamma-COP, Sec21p, a second binding site is proposed to exist on the gamma-COP appendage that interacts with the alpha,beta',epsilon COPI subcomplex.

PubMed: 14690497
DOI: 10.1111/j.1600-0854.2004.00158.x

Experimental method

X-RAY DIFFRACTION (1.9 Å)