3DOE

Complex of ARL2 and BART, Crystal Form 1

3DOE の概要

• エントリーDOI: 10.2210/pdb3doe/pdb
• 関連するPDBエントリー: 3DOF
• 分子名称: ADP-ribosylation factor-like protein 2, ADP-ribosylation factor-like protein 2-binding protein, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: adp-ribosylation factor-like 2, binder of arl2, small gtpase, effector, complex structure, gtp-binding, lipoprotein, myristate, nucleotide-binding, polymorphism, alternative splicing, cytoplasm, mitochondrion, phosphoprotein, signaling protein-hydrolase complex, signaling protein/hydrolase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Mitochondrion intermembrane space: P36404; Cytoplasm: Q9Y2Y0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41503.81

構造登録者

Zhang, T.,Li, S.,Ding, J. (登録日: 2008-07-04, 公開日: 2009-03-03, 最終更新日: 2023-11-01)

主引用文献

Zhang, T.,Li, S.,Zhang, Y.,Zhong, C.,Lai, Z.,Ding, J.
Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector
Structure, 17:602-610, 2009

PubMed Abstract: ARL2 is a member of the ADP-ribosylation factor family but has unique biochemical features. BART is an effector of ARL2 that is essential for nuclear retention of STAT3 and may also be involved in mitochondria transport and apoptosis. Here we report the crystal structure and biochemical characterization of human ARL2-GTP-BART complex. ARL2-GTP assumes a typical small GTPase fold with a unique N-terminal alpha helix conformation. BART consists of a six alpha helix bundle. The interactions between ARL2 and BART involve two interfaces: a conserved N-terminal LLXIL motif of ARL2 is embedded in a hydrophobic cleft of BART and the switch regions of ARL2 interact with helix alpha3 of BART. Both interfaces are essential for the binding as verified by mutagenesis study. This novel recognition and binding mode is different from that of other small GTPase-effector interactions and provides molecular basis for the high specificity of ARL2 for BART.

PubMed: 19368893
DOI: 10.1016/j.str.2009.01.014

実験手法

X-RAY DIFFRACTION (2.25 Å)