2KSQ

The myristoylated yeast ARF1 in a GTP and bicelle bound conformation

2KSQ の概要

• エントリーDOI: 10.2210/pdb2ksq/pdb
• 分子名称: ADP-ribosylation factor 1, S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate, GUANOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: arf, myristoylated, myristoyl, gtp, bicelle, er-golgi transport, golgi apparatus, gtp-binding, lipoprotein, myristate, nucleotide-binding, protein transport, transport, transport protein
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Golgi apparatus: P11076
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22360.67

構造登録者

Liu, Y.,Kahn, R.,Prestegard, J. (登録日: 2010-01-12, 公開日: 2010-07-07, 最終更新日: 2025-03-26)

主引用文献

Liu, Y.,Kahn, R.A.,Prestegard, J.H.
Dynamic structure of membrane-anchored Arf*GTP.
Nat.Struct.Mol.Biol., 17:876-881, 2010

PubMed Abstract: ADP ribosylation factors (Arfs) are N-myristoylated GTP/GDP switch proteins that have key regulatory roles in vesicle transport in eukaryotic cells. ARFs execute their roles by anchoring to membrane surfaces, where they interact with other proteins to initiate budding and maturation of transport vesicles. However, existing structures of Arf*GTP are limited to nonmyristoylated and truncated forms with impaired membrane binding. We report a high-resolution NMR structure for full-length myristoylated yeast (Saccharomyces cerevisiae) Arf1 in complex with a membrane mimic. The two-domain structure, in which the myristoylated N-terminal helix is separated from the C-terminal domain by a flexible linker, suggests a level of adaptability in binding modes for the myriad of proteins with which Arf interacts and allows predictions of specific lipid binding sites on some of these proteins.

PubMed: 20601958
DOI: 10.1038/nsmb.1853

実験手法

SOLUTION NMR