1o3x
From Proteopedia
(New page: 200px<br /> <applet load="1o3x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o3x, resolution 2.10Å" /> '''Crystal structure o...) |
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caption="1o3x, resolution 2.10Å" /> | caption="1o3x, resolution 2.10Å" /> | ||
'''Crystal structure of human GGA1 GAT domain'''<br /> | '''Crystal structure of human GGA1 GAT domain'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1O3X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure superseeds the now removed PDB entry 1J2H. Full crystallographic information is available from [http:// | + | 1O3X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure superseeds the now removed PDB entry 1J2H. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O3X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein transport]] | [[Category: protein transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:32:04 2008'' |
Revision as of 14:32, 15 February 2008
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Crystal structure of human GGA1 GAT domain
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
1O3X is a Single protein structure of sequence from Homo sapiens. This structure superseeds the now removed PDB entry 1J2H. 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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