1pzd
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1pzd |SIZE=350|CAPTION= <scene name='initialview01'>1pzd</scene>, resolution 2.31Å | |PDB= 1pzd |SIZE=350|CAPTION= <scene name='initialview01'>1pzd</scene>, resolution 2.31Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= COPG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |GENE= COPG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pzd OCA], [http://www.ebi.ac.uk/pdbsum/1pzd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pzd RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Hoffman, G R.]] | [[Category: Hoffman, G R.]] | ||
[[Category: Rahl, P B.]] | [[Category: Rahl, P B.]] | ||
| - | [[Category: SO4]] | ||
[[Category: appendage domain]] | [[Category: appendage domain]] | ||
[[Category: ear domain]] | [[Category: ear domain]] | ||
[[Category: platform domain]] | [[Category: platform domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:06:41 2008'' |
Revision as of 20:06, 30 March 2008
| |||||||
| , 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
