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1pzd
From Proteopedia
(New page: 200px<br /><applet load="1pzd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pzd, resolution 2.31Å" /> '''Structural Identific...) |
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| - | [[Image:1pzd.gif|left|200px]]<br /><applet load="1pzd" size=" | + | [[Image:1pzd.gif|left|200px]]<br /><applet load="1pzd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pzd, resolution 2.31Å" /> | caption="1pzd, resolution 2.31Å" /> | ||
'''Structural Identification of a conserved appendage domain in the carboxyl-terminus of the COPI gamma-subunit.'''<br /> | '''Structural Identification of a conserved appendage domain in the carboxyl-terminus of the COPI gamma-subunit.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The formation of coated vesicles is a fundamental step in many | + | 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== | ==About this Structure== | ||
| - | 1PZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1PZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cerione, R | + | [[Category: Cerione, R A.]] |
| - | [[Category: Collins, R | + | [[Category: Collins, R N.]] |
| - | [[Category: Hoffman, G | + | [[Category: Hoffman, G R.]] |
| - | [[Category: Rahl, P | + | [[Category: Rahl, P B.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: appendage domain]] | [[Category: appendage domain]] | ||
| Line 22: | Line 22: | ||
[[Category: platform domain]] | [[Category: platform domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:11 2008'' |
Revision as of 12:34, 21 February 2008
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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 with as ligand. 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 Thu Feb 21 14:34:11 2008
