1o3y: Difference between revisions

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New page: left|200px<br /><applet load="1o3y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o3y, resolution 1.50Å" /> '''Crystal structure of...
 
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[[Image:1o3y.jpg|left|200px]]<br /><applet load="1o3y" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1o3y.jpg|left|200px]]<br /><applet load="1o3y" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1o3y, resolution 1.50&Aring;" />
caption="1o3y, resolution 1.50&Aring;" />
'''Crystal structure of mouse ARF1 (delta17-Q71L), GTP form'''<br />
'''Crystal structure of mouse ARF1 (delta17-Q71L), GTP form'''<br />


==Overview==
==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.
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==
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].  
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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