1pzd

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(New page: 200px<br /><applet load="1pzd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pzd, resolution 2.31&Aring;" /> '''Structural Identific...)
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[[Image:1pzd.gif|left|200px]]<br /><applet load="1pzd" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pzd.gif|left|200px]]<br /><applet load="1pzd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pzd, resolution 2.31&Aring;" />
caption="1pzd, resolution 2.31&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PZD OCA].
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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]]
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[[Category: Cerione, R.A.]]
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[[Category: Cerione, R A.]]
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[[Category: Collins, R.N.]]
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[[Category: Collins, R N.]]
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[[Category: Hoffman, G.R.]]
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[[Category: Hoffman, G R.]]
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[[Category: Rahl, P.B.]]
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[[Category: Rahl, P B.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: appendage domain]]
[[Category: appendage domain]]
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[[Category: platform domain]]
[[Category: platform domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:15:33 2007''
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''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


1pzd, resolution 2.31Å

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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

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