4DVG

Crystal structure of E. histolytica Formin1 bound to EhRho1-GTPgammaS

4DVG の概要

• エントリーDOI: 10.2210/pdb4dvg/pdb
• 関連するPDBエントリー: 3REF 3REG
• 分子名称: Rho-like small GTPase, Diaphanous protein, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: cytoskeleton, armadillo repeat, gtpase-binding domain, nucleotide-binding, signaling protein, lipoprotein, actin filament formation, prenylation, gtp binding-actin binding proteins complex, gtp binding/actin binding proteins
• 由来する生物種: Entamoeba histolytica; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62613.19

構造登録者

Bosch, D.E.,Siderovski, D.P. (登録日: 2012-02-23, 公開日: 2012-11-14, 最終更新日: 2024-11-20)

主引用文献

Bosch, D.E.,Yang, B.,Siderovski, D.P.
Entamoeba histolytica Rho1 Regulates Actin Polymerization through a Divergent, Diaphanous-Related Formin.
Biochemistry, 51:8791-8801, 2012

PubMed Abstract: Entamoeba histolytica requires a dynamic actin cytoskeleton for intestinal and systemic pathogenicity. Diaphanous-related formins represent an important family of actin regulators that are activated by Rho GTPases. The E. histolytica genome encodes a large family of Rho GTPases and three diaphanous-related formins, of which EhFormin1 is known to regulate mitosis and cytokinesis in trophozoites. We demonstrate that EhFormin1 modulates actin polymerization through its formin homology 2 domain. Despite a highly divergent diaphanous autoinhibitory domain, EhFormin1 is autoinhibited by an N- and C-terminal intramolecular interaction but activated upon binding of EhRho1 to the N-terminal domain tandem. A crystal structure of the EhRho1·GTPγS-EhFormin1 complex illustrates an EhFormin1 conformation that diverges from mammalian mDia1 and lacks a secondary interaction with a Rho insert helix. The structural model also highlights residues required for specific recognition of the EhRho1 GTPase and suggests that the molecular mechanisms of EhFormin1 autoinhibition and activation differ from those of mammalian homologues.

PubMed: 23050667
DOI: 10.1021/bi300954g

実験手法

X-RAY DIFFRACTION (2.604 Å)