The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms
- 1 September 1995
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 2 (9), 797-806
- https://doi.org/10.1038/nsb0995-797
Abstract
The ARFs are a family of 21,000 M(r) proteins with biological roles in constitutive secretion and activation of phospholipase D. The structure of ARF-1 complexed to GDP determined from two crystal forms reveals a topology that is similar to that of the protein p21 ras with two differences: an additional amino-terminal helix and an extra beta-strand. The Mg2+ ion in ARF-1 displays a five-coordination sphere; this feature is not seen in p21 ras, due to a shift in the relative position of the DXXG motif between the two proteins. The occurrence of a dimer in one crystal form suggests that ARF-1 may dimerize during its biological function. The dimer interface involves a region of the ARF-1 molecule that is analogous to the effector domain in p21 ras and may mediate interactions with its effectors.Keywords
This publication has 35 references indexed in Scilit:
- ADP-ribosylation Factor-directed GTPase-activating ProteinPublished by Elsevier ,1995
- Mechanisms of intracellular protein transportNature, 1994
- ARF: a key regulatory switch in membrane traffic and organelle structureCurrent Opinion in Cell Biology, 1994
- Identification of a brefeldin A-insensitive guanine nucleotide-exchange protein for ADP-ribosylation factor in bovine brain.Proceedings of the National Academy of Sciences, 1994
- Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles.The Journal of cell biology, 1993
- Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosolNature, 1993
- ADP-ribosylation factors, 20,000 Mr guanine nucleotide-binding protein activators of cholera toxin and components of intracellular vesicular transport systemsCellular Signalling, 1993
- Two distinct populations of ARF bound to Golgi membranes.The Journal of cell biology, 1993
- ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes.Proceedings of the National Academy of Sciences, 1992
- ADP-Ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding proteinCell, 1991