2j5x
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The small GTP-binding protein Arf6 coordinates membrane traffic at the | + | The small GTP-binding protein Arf6 coordinates membrane traffic at the plasma membrane with aspects of cytoskeleton organization. This function does not overlap with that of other members of the ADP-ribosylation factor (Arf) family, although their switch regions, which are their major sites of interaction with regulators and effectors, have virtually identical sequences. Here we report the crystal structure of full-length, non-myristoylated human Arf6 bound to GTPgammaS. Unlike their GDP-bound forms, the active forms of Arf6 and Arf1 are very similar. Thus, the switch regions are discriminatory elements between Arf isoforms in their inactive but not in their active forms, a property that may generalize to other families of small G proteins. This suggests that GTP-bound Arfs may establish specific interactions outside the switch regions and/or be recognized in their cellular context rather than as isolated proteins. The structure also allows further insight into the lack of spontaneous GTPase activity of Arf proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 2J5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GSP:'>GSP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 2J5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GSP:'>GSP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1HFV. Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J5X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:59:32 2008'' |
Revision as of 15:59, 21 February 2008
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STRUCTURE OF THE SMALL G PROTEIN ARF6 IN COMPLEX WITH GTPGAMMAS
Overview
The small GTP-binding protein Arf6 coordinates membrane traffic at the plasma membrane with aspects of cytoskeleton organization. This function does not overlap with that of other members of the ADP-ribosylation factor (Arf) family, although their switch regions, which are their major sites of interaction with regulators and effectors, have virtually identical sequences. Here we report the crystal structure of full-length, non-myristoylated human Arf6 bound to GTPgammaS. Unlike their GDP-bound forms, the active forms of Arf6 and Arf1 are very similar. Thus, the switch regions are discriminatory elements between Arf isoforms in their inactive but not in their active forms, a property that may generalize to other families of small G proteins. This suggests that GTP-bound Arfs may establish specific interactions outside the switch regions and/or be recognized in their cellular context rather than as isolated proteins. The structure also allows further insight into the lack of spontaneous GTPase activity of Arf proteins.
About this Structure
2J5X is a Single protein structure of sequence from Homo sapiens with and as ligands. This structure supersedes the now removed PDB entry 1HFV. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The structural GDP/GTP cycle of human Arf6., Pasqualato S, Menetrey J, Franco M, Cherfils J, EMBO Rep. 2001 Mar;2(3):234-8. PMID:11266366
Page seeded by OCA on Thu Feb 21 17:59:32 2008
Categories: Homo sapiens | Single protein | Cherfils, J. | Franco, M. | Menetrey, J. | Pasqualato, S. | GSP | MG | Arf | Arf6 | Er-golgi transport | G protein | Golgi apparatus | Gtp-binding | Lipoprotein | Membrane traffic | Myristate | Nucleotide-binding | Protein transport | Ras | Transport
