1HUR

HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED

1HUR の概要

• エントリーDOI: 10.2210/pdb1hur/pdb
• 分子名称: HUMAN ADP-RIBOSYLATION FACTOR 1, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: gdp-binding, membrane traffickin, non-myristoylated, protein transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Golgi apparatus: P84077
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42116.11

構造登録者

Amor, J.C.,Harrison, D.H.,Kahn, R.A.,Ringe, D. (登録日: 1995-04-19, 公開日: 1995-07-10, 最終更新日: 2024-02-07)

主引用文献

Amor, J.C.,Harrison, D.H.,Kahn, R.A.,Ringe, D.
Structure of the human ADP-ribosylation factor 1 complexed with GDP.
Nature, 372:704-708, 1994

PubMed Abstract: ADP-ribosylation factors (ARFs) are essential and ubiquitous in eukaryotes, being involved in vesicular transport and functioning as an activator of phospholipase D (refs 1, 2) and cholera toxin. The functions of ARF proteins in membrane traffic and organelle integrity are intimately tied to its reversible association with membranes and specific interactions with membrane phospholipids. One common feature of these functions is their regulation by the binding and hydrolysis of GTP. Here we report the three-dimensional structure of full-length human ARF1 (M(r) 21,000) in its GDP-bound non-myristoylated form. The presence of a unique amino-terminal alpha-helix and loop, together with differences in Mg2+ ligation and the existence of a non-crystallographic dimer, set this structure apart from other GTP-binding proteins. These features provide a structural basis for the GTP-dependent modulation of membrane affinity, the lack of intrinsic GTPase activity, and the nature of effector binding surfaces.

PubMed: 7990966
DOI: 10.1038/372704a0

実験手法

X-RAY DIFFRACTION (2 Å)