Summary for 2J5X
| Entry DOI | 10.2210/pdb2j5x/pdb |
| Related | 1E0S 2A5D 2A5F 2A5G |
| Descriptor | ADP-RIBOSYLATION FACTOR 6, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | membrane traffic, protein transport, ras, arf, arf6, g protein, myristate, transport, er-golgi transport, nucleotide-binding, lipoprotein, gtp-binding, golgi apparatus |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Golgi apparatus: P62330 |
| Total number of polymer chains | 2 |
| Total formula weight | 41347.43 |
| Authors | Pasqualato, S.,Menetrey, J.,Franco, M.,Cherfils, J. (deposition date: 2006-09-20, release date: 2006-09-21, Last modification date: 2024-05-01) |
| Primary citation | Pasqualato, S.,Menetrey, J.,Franco, M.,Cherfils, J. The Structural Gdp-GTP Cycle of Human Arf6. Embo Rep., 2:234-, 2001 Cited by PubMed Abstract: 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. PubMed: 11266366DOI: 10.1093/EMBO-REPORTS/KVE043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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