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1pzd
From Proteopedia
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| , resolution 2.31Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | COPG (Bos taurus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structural Identification of a conserved appendage domain in the carboxyl-terminus of the COPI gamma-subunit.
Overview
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.
About this Structure
1PZD is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Conserved structural motifs in intracellular trafficking pathways: structure of the gammaCOP appendage domain., Hoffman GR, Rahl PB, Collins RN, Cerione RA, Mol Cell. 2003 Sep;12(3):615-25. PMID:14527408
Page seeded by OCA on Sun Mar 30 23:06:41 2008
