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ADP-ribosylation factor-like 1 (ARL1) from Saccharomyces cerevisiae
Structural highlights
FunctionARL1_YEAST Recruits golgins such as IMH1 to the Golgi. Can bind and hydrolyze GTP. May be involved in trafficking events within the endosomal system.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStructures 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. Structures of yeast ARF2 and ARL1: distinct roles for the N terminus in the structure and function of ARF family GTPases.,Amor JC, Horton JR, Zhu X, Wang Y, Sullards C, Ringe D, Cheng X, Kahn RA J Biol Chem. 2001 Nov 9;276(45):42477-84. Epub 2001 Sep 4. PMID:11535602[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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