Structure of the human ADP-ribosylation factor 1 complexed with GDP

@article{Amor1994StructureOT,
  title={Structure of the human ADP-ribosylation factor 1 complexed with GDP},
  author={Juan Carlos Amor and David H. T. Harrison and Richard A. Kahn and Dagmar Ringe},
  journal={Nature},
  year={1994},
  volume={372},
  pages={704-708}
}
ADP-ribosylation factors (ARFs) are essential and ubiquitous in eukaryotes, being involved in vesicular transport and functioning as an activator of phospholipase D (refs 1,2) and cholera toxin3,4. The functions of ARF proteins in membrane traffic and organelle integrity5,6 are intimately tied to its reversible association with membranes and specific interactions with membrane phospholipids. One common feature of these functions is their regulation by the binding and hydrolysis of GTP. Here we… 
Dual Interaction of ADP Ribosylation Factor 1 with Sec7 Domain and with Lipid Membranes during Catalysis of Guanine Nucleotide Exchange*
TLDR
The results suggest that the conformational switch of the N-terminal helix of myrARF1 to the membrane-bound form is an early event in the nucleotide exchange pathway and is a prerequisite for a structural rearrangement at the myr ARF1-GDP/Sec7 domain interface that allows the glutamic finger to expel GDP from myrarF1.
The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms
TLDR
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 β-strand.
Different Domains of Mammalian ADP-ribosylation Factor 1 Mediate Interaction with Selected Target Proteins*
TLDR
Since residues 35–94 of mARF1 are critical for optimal activity in both PLD1 activation and AP-1 recruitment, it is hypothesize that this region of ARF contains residues that interact with effector molecules.
Characterization of a GDP Dissociation Inhibitory Region of ADP-ribosylation Factor Domain Protein ARD1*
TLDR
It was demonstrated that the 15 amino acids directly preceding the ARF domain were responsible for decreasing the rate of GDP dissociation but not guanosine 5-[γ-thio]triphosphate dissociation, and suggested that, like the amino-terminal segment of ARF, the equivalent region in ARD1, located between the GTPase-activating protein and ARF domains, may act as a GDP Dissociation inhibitor.
Activation of toxin ADP-ribosyltransferases by eukaryotic ADP-ribosylation factors
TLDR
Sequences of peptides from a BFA-sensitive GEP purified in the laboratory revealed the presence of a Sec7 domain, a sequence of ~200 amino acids that resembles a region in the yeast Sec7 gene product, which is involved in Golgi vesicular transport.
Dynamic structure of membrane-anchored Arf•GTP
TLDR
A high-resolution NMR structure for full-length myristoylated yeast (Saccharomyces cerevisiae) Arf1 in complex with a membrane mimic suggests a level of adaptability in binding modes for the myriad of proteins with which Arf interacts and allows predictions of specific lipid binding sites on some of these proteins.
Activation of toxin ADP-ribosyltransferases by eukaryotic ADP-ribosylation factors
TLDR
Sequences of peptides from a BFA-sensitive GEP purified in the laboratory revealed the presence of a Sec7 domain, a sequence of ~200 amino acids that resembles a region in the yeast Sec7 gene product, which is involved in Golgi vesicular transport.
Structure and membrane interaction of myristoylated ARF1.
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References

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Sequences of the bovine and yeast ADP-ribosylation factor and comparison to other GTP-binding proteins.
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  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1988
TLDR
Comparison of the cDNA-derived amino acid sequences of ARF to other GTP-binding proteins reveals a structural relationship between ARF and the ras family of proteins, and comparison of the ARF sequences to that of the chicken processed pseudogene reveals that CPS-1 is actually an ARF-derived gene.
Refined structure of elongation factor EF-Tu from Escherichia coli.
Role of glutamine-61 in the hydrolysis of GTP by p21H-ras: an experimental and theoretical study.
TLDR
Under saturating concentrations of GTP the Q61E mutant of p21H-ras has a 20-fold greater rate of intrinsic hydrolysis than the wild type, and the residue 61 side chain in transient contact with a water molecule that is well-positioned for hydrolytic attack on the gamma phosphate.
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