1o3y

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(New page: 200px<br /><applet load="1o3y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o3y, resolution 1.50&Aring;" /> '''Crystal structure of...)
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'''Crystal structure of mouse ARF1 (delta17-Q71L), GTP form'''<br />
'''Crystal structure of mouse ARF1 (delta17-Q71L), GTP form'''<br />
==Overview==
==Overview==
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GGAs are critical for trafficking soluble proteins from the trans-Golgi, network (TGN) to endosomes/lysosomes through interactions with TGN-sorting, receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to, TGN membranes recruits its effector GGA by binding to the GAT domain, thus, facilitating recognition of GGA for cargo-loaded receptors. Here we report, the X-ray crystal structures of the human GGA1-GAT domain and the complex, between ARF1-GTP and the N-terminal region of the GAT domain. When, unbound, the GAT domain forms an elongated bundle of three a-helices with, a hydrophobic core. Structurally, this domain, combined with the preceding, VHS domain, resembles CALM, an AP180 homolog involved in endocytosis. In, the complex with ARF1-GTP, a helix-loop-helix of the N-terminal part of, GGA1-GAT interacts with the switches 1 and 2 of ARF1 predominantly in a, hydrophobic manner. These data reveal a molecular mechanism underlying, membrane recruitment of adaptor proteins by ARF-GTP.
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GGAs are critical for trafficking soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes through interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to TGN membranes recruits its effector GGA by binding to the GAT domain, thus facilitating recognition of GGA for cargo-loaded receptors. Here we report the X-ray crystal structures of the human GGA1-GAT domain and the complex between ARF1-GTP and the N-terminal region of the GAT domain. When unbound, the GAT domain forms an elongated bundle of three a-helices with a hydrophobic core. Structurally, this domain, combined with the preceding VHS domain, resembles CALM, an AP180 homolog involved in endocytosis. In the complex with ARF1-GTP, a helix-loop-helix of the N-terminal part of GGA1-GAT interacts with the switches 1 and 2 of ARF1 predominantly in a hydrophobic manner. These data reveal a molecular mechanism underlying membrane recruitment of adaptor proteins by ARF-GTP.
==About this Structure==
==About this Structure==
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1O3Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1J2I. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O3Y OCA].
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1O3Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1J2I. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O3Y OCA].
==Reference==
==Reference==
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[[Category: protein transport]]
[[Category: protein transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:49:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:13:17 2008''

Revision as of 12:13, 21 February 2008

Image:1o3y.jpg

1o3y, resolution 1.50Å

Drag the structure with the mouse to rotate

Crystal structure of mouse ARF1 (delta17-Q71L), GTP form

Overview

GGAs are critical for trafficking soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes through interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to TGN membranes recruits its effector GGA by binding to the GAT domain, thus facilitating recognition of GGA for cargo-loaded receptors. Here we report the X-ray crystal structures of the human GGA1-GAT domain and the complex between ARF1-GTP and the N-terminal region of the GAT domain. When unbound, the GAT domain forms an elongated bundle of three a-helices with a hydrophobic core. Structurally, this domain, combined with the preceding VHS domain, resembles CALM, an AP180 homolog involved in endocytosis. In the complex with ARF1-GTP, a helix-loop-helix of the N-terminal part of GGA1-GAT interacts with the switches 1 and 2 of ARF1 predominantly in a hydrophobic manner. These data reveal a molecular mechanism underlying membrane recruitment of adaptor proteins by ARF-GTP.

About this Structure

1O3Y is a Single protein structure of sequence from Mus musculus with and as ligands. This structure supersedes the now removed PDB entry 1J2I. Full crystallographic information is available from OCA.

Reference

Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport., Shiba T, Kawasaki M, Takatsu H, Nogi T, Matsugaki N, Igarashi N, Suzuki M, Kato R, Nakayama K, Wakatsuki S, Nat Struct Biol. 2003 May;10(5):386-93. PMID:12679809

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