1MR3
Saccharomyces cerevisiae ADP-ribosylation Factor 2 (ScArf2) complexed with GDP-3'P at 1.6A resolution
Summary for 1MR3
| Entry DOI | 10.2210/pdb1mr3/pdb |
| Related | 1hur |
| Descriptor | ADP-ribosylation factor 2, MAGNESIUM ION, GUANOSINE-3'-MONOPHOSPHATE-5'-DIPHOSPHATE, ... (8 entities in total) |
| Functional Keywords | gtp-binding, gdp-3'phosphate, small gtpase, signal transduction, signaling protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Golgi apparatus : P19146 |
| Total number of polymer chains | 1 |
| Total formula weight | 22369.38 |
| Authors | Amor, J.-C.,Horton, J.R.,Zhu, X.,Wang, Y.,Sullards, C.,Ringe, D.,Cheng, X.,Kahn, R.A. (deposition date: 2002-09-17, release date: 2002-11-20, Last modification date: 2024-02-14) |
| 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 Cited by 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: 11535602DOI: 10.1074/jbc.M106660200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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