TY - JOUR
T1 - Structures of Yeast ARF2 and ARL1. Distinct roles for the N terminus in the structure and function of ARF family GTPases
AU - Amor, J. Carlos
AU - Horton, John R.
AU - Zhu, Xinjun
AU - Wang, Yi
AU - Sullards, Cameron
AU - Ringe, Dagmar
AU - Cheng, Xiaodong
AU - Kahn, Richard A.
PY - 2001/11/9
Y1 - 2001/11/9
N2 - Structures were determined by x-ray crystallography for two members of the ADP-ribosylation factor (ARF) family of regulatory GTPases, yeast ARF1 and ARL1, and were compared with 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 α-helix, switch I, and the interswitch region, which along with differences in surface electrostatics provide explanations for the different biophysical and biochemical properties of ARF and ARF-like proteins.
AB - Structures were determined by x-ray crystallography for two members of the ADP-ribosylation factor (ARF) family of regulatory GTPases, yeast ARF1 and ARL1, and were compared with 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 α-helix, switch I, and the interswitch region, which along with differences in surface electrostatics provide explanations for the different biophysical and biochemical properties of ARF and ARF-like proteins.
UR - http://www.scopus.com/inward/record.url?scp=0035834688&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035834688&partnerID=8YFLogxK
U2 - 10.1074/jbc.M106660200
DO - 10.1074/jbc.M106660200
M3 - Article
C2 - 11535602
AN - SCOPUS:0035834688
SN - 0021-9258
VL - 276
SP - 42477
EP - 42484
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 45
ER -