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Papers In Press, published online ahead of print September 4, 2001
Department of Biochemistry, Emory University, Atlanta, GA 30322-3050
Corresponding Author: rkahn{at}emory.edu
Structures were determined by x-ray crystallography for two members of the ARF family of regulatory GTPases, yeast ARF1 and ARL1, and were compared to previously determined structures of human ARF1 and ARF6. These analyses revealed an overall conserved fold but differences in primary sequence and length, particularly in an N-terminal loop, lead to differences in nucleotide and divalent metal binding. Packing of hydrophobic residues is central to the interplay between the N-terminal "-helix, switch I, and the inter-switch region, which along with differences in surface electrostatics provide explanations for the different biophysical and biochemical properties of ARF and ARL proteins.
J. Biol. Chem, 10.1074/jbc.M106660200
Submitted on July 16, 2001
Revised on September 4, 2001
Accepted on September 4, 2001
Structures of yeast ARF2 and ARL1: distinct roles for the N-terminus in the structure and function of ARF family GTPases
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