2J59

Crystal structure of the ARF1:ARHGAP21-ArfBD complex

2J59 の概要

• エントリーDOI: 10.2210/pdb2j59/pdb
• 関連するPDBエントリー: 1O3Y
• 分子名称: ADP-RIBOSYLATION FACTOR 1, RHO-GTPASE ACTIVATING PROTEIN 10, GUANOSINE-5'-TRIPHOSPHATE, ... (8 entities in total)
• 機能のキーワード: arf, arf1, arfbd, arhgap21, myristate, transport, nucleotide-binding, rhogap protein, hydrolase, protein transport, actin organization, small gtp-binding protein, golgi apparatus
• 由来する生物種: MUS MUSCULUS (MOUSE); 詳細
• 細胞内の位置: Golgi apparatus: P84078
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 234295.03

構造登録者

Menetrey, J.,Perderiset, M.,Cicolari, J.,Dubois, T.,El Khatib, N.,El Khadali, F.,Franco, M.,Chavrier, P.,Houdusse, A. (登録日: 2006-09-13, 公開日: 2007-02-20, 最終更新日: 2023-12-13)

主引用文献

Menetrey, J.,Perderiset, M.,Cicolari, J.,Dubois, T.,El Khatib, N.,El Khadali, F.,Franco, M.,Chavrier, P.,Houdusse, A.
Structural Basis for Arf1-Mediated Recruitment of Arhgap21 to Golgi Membranes.
Embo J., 26:1953-, 2007

PubMed Abstract: ARHGAP21 is a Rho family GTPase-activating protein (RhoGAP) that controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. ARHGAP21 is recruited to the Golgi by binding to another small GTPase, ARF1. Here, we present the crystal structure of the activated GTP-bound form of ARF1 in a complex with the Arf-binding domain (ArfBD) of ARHGAP21 at 2.1 A resolution. We show that ArfBD comprises a PH domain adjoining a C-terminal alpha helix, and that ARF1 interacts with both of these structural motifs through its switch regions and triggers structural rearrangement of the PH domain. We used site-directed mutagenesis to confirm that both the PH domain and the helical motif are essential for the binding of ArfBD to ARF1 and for its recruitment to the Golgi. Our data demonstrate that two well-known small GTPase-binding motifs, the PH domain and the alpha helical motif, can combine to create a novel mode of binding to Arfs.

PubMed: 17347647
DOI: 10.1038/SJ.EMBOJ.7601634

実験手法

X-RAY DIFFRACTION (2.1 Å)