1j2j
From Proteopedia
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|PDB= 1j2j |SIZE=350|CAPTION= <scene name='initialview01'>1j2j</scene>, resolution 1.60Å | |PDB= 1j2j |SIZE=350|CAPTION= <scene name='initialview01'>1j2j</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GTP:GUANOSINE-5'-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1j2h|1J2H]], [[1j2i|1J2I]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2j OCA], [http://www.ebi.ac.uk/pdbsum/1j2j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j2j RCSB]</span> | ||
}} | }} | ||
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[[Category: Takatsu, H.]] | [[Category: Takatsu, H.]] | ||
[[Category: Wakatsuki, S.]] | [[Category: Wakatsuki, S.]] | ||
| - | [[Category: GTP]] | ||
| - | [[Category: IOD]] | ||
| - | [[Category: MG]] | ||
[[Category: protein transport]] | [[Category: protein transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:27:59 2008'' |
Revision as of 18:28, 30 March 2008
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| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1J2H, 1J2I
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of GGA1 GAT N-terminal region in complex with ARF1 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
1J2J is a Protein complex structure of sequences from Homo sapiens and Mus musculus. 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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