1MOZ

ADP-ribosylation factor-like 1 (ARL1) from Saccharomyces cerevisiae

Summary for 1MOZ

• Entry DOI: 10.2210/pdb1moz/pdb
• Related: 1HUR 1RRF
• Descriptor: ADP-ribosylation factor-like protein 1, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: gtp-binding, protein binding
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Golgi apparatus : P38116
• Total number of polymer chains: 2
• Total formula weight: 41795.06

Authors

Amor, J.C.,Horton, J.R.,Zhu, X.,Wang, Y.,Sullards, C.,Ringe, D.,Cheng, X.,Kahn, R.A. (deposition date: 2002-09-10, release date: 2002-10-09, Last modification date: 2017-10-11)

Primary citation

Amor, J.C.,Horton, J.R.,Zhu, X.,Wang, Y.,Sullards, C.,Ringe, D.,Cheng, X.,Kahn, R.A.
Structures of Yeast ARF2 and ARL1: DISTINCT ROLES FOR THE N TERMINUS IN THE STRUCTURE AND FUNCTION OF ARF FAMILY GTPases
J.Biol.Chem., 276:42477-42484, 2001

PubMed 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.

PubMed: 11535602
DOI: 10.1074/jbc.M106660200

Experimental method

X-RAY DIFFRACTION (3.17 Å)