Structures of yeast ARF2 and ARL1: distinct roles for the N terminus in the structure and function of ARF family GTPases.

@article{citeulike:2883883, abstract = {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 alpha-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.}, address = {Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322-3050, USA.}, author = {Amor, J. C. and Horton, J. R. and Zhu, X. and Wang, Y. and Sullards, C. and Ringe, D. and Cheng, X. and Kahn, R. A. }, citeulike-article-id = {2883883}, doi = {http://dx.doi.org/10.1074/jbc.M106660200}, issn = {0021-9258}, journal = {The Journal of biological chemistry}, keywords = {arf, arl}, month = {November}, number = {45}, pages = {42477--42484}, posted-at = {2008-06-11 22:46:04}, priority = {2}, title = {Structures of yeast ARF2 and ARL1: distinct roles for the N terminus in the structure and function of ARF family GTPases.}, url = {http://dx.doi.org/10.1074/jbc.M106660200}, volume = {276}, year = {2001} }

TY - JOUR ID - citeulike:2883883 L3 - citeulike-article-id:2883883 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 alpha-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. IS - 45 JF - The Journal of biological chemistry SN - 0021-9258 AD - Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322-3050, USA. EP - 42484 TI - Structures of yeast ARF2 and ARL1: distinct roles for the N terminus in the structure and function of ARF family GTPases. VL - 276 SP - 42477 KW - arf KW - arl AU - Amor, JC AU - Horton, JR AU - Zhu, X AU - Wang, Y AU - Sullards, C AU - Ringe, D AU - Cheng, X AU - Kahn, RA PY - 2001/11/09/ UR - http://dx.doi.org/10.1074/jbc.M106660200 ER -