3TJZ

Crystal Structure of Arf1 Bound to the gamma/zeta-COP Core Complex

Summary for 3TJZ

• Entry DOI: 10.2210/pdb3tjz/pdb
• Descriptor: ADP-ribosylation factor 1, Coatomer subunit gamma, Coatomer subunit zeta-1, ... (5 entities in total)
• Functional Keywords: protein trafficking, golgi membrane, protein transport-protein binding complex, protein transport/protein binding
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Golgi apparatus: P11076; Cytoplasm: P53620; Cytoplasm (By similarity): P35604
• Total number of polymer chains: 6
• Total formula weight: 152134.40

Authors

Goldberg, J.,Yu, X.,Breitman, M. (deposition date: 2011-08-25, release date: 2012-02-22, Last modification date: 2024-02-28)

Primary citation

Yu, X.,Breitman, M.,Goldberg, J.
A structure-based mechanism for arf1-dependent recruitment of coatomer to membranes.
Cell(Cambridge,Mass.), 148:530-542, 2012

PubMed Abstract: Budding of COPI-coated vesicles from Golgi membranes requires an Arf family G protein and the coatomer complex recruited from cytosol. Arf is also required with coatomer-related clathrin adaptor complexes to bud vesicles from the trans-Golgi network and endosomal compartments. To understand the structural basis for Arf-dependent recruitment of a vesicular coat to the membrane, we determined the structure of Arf1 bound to the γζ-COP subcomplex of coatomer. Structure-guided biochemical analysis reveals that a second Arf1-GTP molecule binds to βδ-COP at a site common to the γ- and β-COP subunits. The Arf1-binding sites on coatomer are spatially related to PtdIns4,5P(2)-binding sites on the endocytic AP2 complex, providing evidence that the orientation of membrane binding is general for this class of vesicular coat proteins. A bivalent GTP-dependent binding mode has implications for the dynamics of coatomer interaction with the Golgi and for the selection of cargo molecules.

PubMed: 22304919
DOI: 10.1016/j.cell.2012.01.015

Experimental method

X-RAY DIFFRACTION (2.9 Å)