1pzd: Difference between revisions
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[[Image:1pzd.gif|left|200px]] | [[Image:1pzd.gif|left|200px]] | ||
'''Structural Identification of a conserved appendage domain in the carboxyl-terminus of the COPI gamma-subunit.''' | {{Structure | ||
|PDB= 1pzd |SIZE=350|CAPTION= <scene name='initialview01'>1pzd</scene>, resolution 2.31Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= COPG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |||
}} | |||
'''Structural Identification of a conserved appendage domain in the carboxyl-terminus of the COPI gamma-subunit.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1PZD is a [ | 1PZD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZD OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14527408 14527408] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: platform domain]] | [[Category: platform domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:30:59 2008'' | ||
Revision as of 11:31, 20 March 2008
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| 1pzd, resolution 2.31Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Gene: | COPG (Bos taurus) | ||||||||||||
| 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
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