4CID

Structural insights into the N-terminus of the EHD2 ATPase

4CID の概要

• エントリーDOI: 10.2210/pdb4cid/pdb
• 分子名称: EH DOMAIN-CONTAINING PROTEIN 2, CALCIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• 機能のキーワード: hydrolase, mechanochemical atpase, dynamin superfamily
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE)
• 細胞内の位置: Cell membrane; Peripheral membrane protein; Cytoplasmic side: Q8BH64
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 63212.85

構造登録者

Shah, C.,Daumke, O. (登録日: 2013-12-06, 公開日: 2014-02-19, 最終更新日: 2024-11-13)

主引用文献

Shah, C.,Hegde, B.G.,Mor, B.,Behrmann, E.,Mielke, T.,Moenke, G.,Spahn, C.M.,Lundmark, R.,Daumke, O.,Langen, R.
Structural Insights Into Membrane Interaction and Caveolar Targeting of Dynamin-Like Ehd2.
Structure, 22:409-, 2014

PubMed Abstract: The dynamin-related Eps15-homology domain-containing protein 2 (EHD2) is a membrane-remodeling ATPase that regulates the dynamics of caveolae. Here, we established an electron paramagnetic resonance (EPR) approach to characterize structural features of membrane-bound EHD2. We show that residues at the tip of the helical domain can insert into the membrane and may create membrane curvature by a wedging mechanism. Using EPR and X-ray crystallography, we found that the N terminus is folded into a hydrophobic pocket of the GTPase domain in solution and can be released into the membrane. Cryoelectron microscopy demonstrated that the N terminus is not essential for oligomerization of EHD2 into a membrane-anchored scaffold. Instead, we found a function of the N terminus in regulating targeting and stable association of EHD2 to caveolae. Our data uncover an unexpected, membrane-induced regulatory switch in EHD2 and demonstrate the versatility of EPR to study structure and function of dynamin superfamily proteins.

PubMed: 24508342
DOI: 10.1016/J.STR.2013.12.015

実験手法

X-RAY DIFFRACTION (3 Å)