1RRG

NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, DIMERIC CRYSTAL FORM

Summary for 1RRG

• Entry DOI: 10.2210/pdb1rrg/pdb
• Descriptor: RAT ADP-RIBOSYLATION FACTOR-1, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: transport protein, gdp-binding, membrane trafficking, homodimer
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Golgi apparatus: P84079
• Total number of polymer chains: 2
• Total formula weight: 42378.50

Authors

Greasley, S.E.,Jhoti, H.,Bax, B. (deposition date: 1995-12-16, release date: 1996-06-20, Last modification date: 2024-02-14)

Primary citation

Greasley, S.E.,Jhoti, H.,Teahan, C.,Solari, R.,Fensome, A.,Thomas, G.M.,Cockcroft, S.,Bax, B.
The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms.
Nat.Struct.Biol., 2:797-806, 1995

PubMed 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.

PubMed: 7552752
DOI: 10.1038/nsb0995-797

Experimental method

X-RAY DIFFRACTION (2.4 Å)