1PZD

Structural Identification of a conserved appendage domain in the carboxyl-terminus of the COPI gamma-subunit.

Summary for 1PZD

• Entry DOI: 10.2210/pdb1pzd/pdb
• Descriptor: Coatomer gamma subunit, SULFATE ION (3 entities in total)
• Functional Keywords: platform domain, appendage domain, ear domain, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm, cytosol: P53620
• Total number of polymer chains: 1
• Total formula weight: 36036.37

Authors

Hoffman, G.R.,Rahl, P.B.,Collins, R.N.,Cerione, R.A. (deposition date: 2003-07-10, release date: 2003-10-14, Last modification date: 2024-02-14)

Primary citation

Hoffman, G.R.,Rahl, P.B.,Collins, R.N.,Cerione, R.A.
Conserved Structural Motifs in Intracellular Trafficking Pathways. Structure of the gammaCOP Appendage Domain.
Mol.Cell, 12:615-625, 2003

PubMed Abstract: The formation of coated vesicles is a fundamental step in many intracellular trafficking pathways. COPI and clathrin represent two important and distinct sets of vesicle coating machinery, involved primarily in mediating intra-Golgi and endocytic transport, respectively. Here we identify an important functional region at the carboxyl terminus of the gamma subunit of the COPI complex (gammaCOP) and describe the X-ray crystal structure of this domain at 2.3 A resolution. This domain of gammaCOP exhibits unexpected structural similarity to the carboxyl-terminal appendage domains of the alpha and beta subunits of the AP2 adaptor proteins, integral components of clathrin-coated vesicles. The remarkable structural conservation exhibited by the gammaCOP appendage domain, coupled with functional data and primary sequence analysis, supports a model of COPI function with significant structural and mechanistic parallels to vesicular transport by the clathrin/AP2 system.

PubMed: 14527408
DOI: 10.1016/j.molcel.2003.08.002

Experimental method

X-RAY DIFFRACTION (2.31 Å)