1MR3

Saccharomyces cerevisiae ADP-ribosylation Factor 2 (ScArf2) complexed with GDP-3'P at 1.6A resolution

1MR3 の概要

• エントリーDOI: 10.2210/pdb1mr3/pdb
• 関連するPDBエントリー: 1hur
• 分子名称: ADP-ribosylation factor 2, MAGNESIUM ION, GUANOSINE-3'-MONOPHOSPHATE-5'-DIPHOSPHATE, ... (8 entities in total)
• 機能のキーワード: gtp-binding, gdp-3'phosphate, small gtpase, signal transduction, signaling protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Golgi apparatus : P19146
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22369.38

構造登録者

Amor, J.-C.,Horton, J.R.,Zhu, X.,Wang, Y.,Sullards, C.,Ringe, D.,Cheng, X.,Kahn, R.A. (登録日: 2002-09-17, 公開日: 2002-11-20, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.6 Å)