3ZEE

Electron cyro-microscopy helical reconstruction of Par-3 N terminal domain

3ZEE の概要

• エントリーDOI: 10.2210/pdb3zee/pdb
• EMDBエントリー: 2237
• 分子名称: PARTITIONING DEFECTIVE 3 HOMOLOG (1 entity in total)
• 機能のキーワード: cell cycle
• 由来する生物種: RATTUS NORVEGICUS (NORWAY RAT)
• 細胞内の位置: Cytoplasm : Q9Z340
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9552.91

構造登録者

Zhang, Y.,Wang, W.,Chen, J.,Zhang, K.,Gao, F.,Gong, W.,Zhang, M.,Sun, F.,Feng, W. (登録日: 2012-12-05, 公開日: 2013-10-16, 最終更新日: 2024-05-08)

主引用文献

Zhang, Y.,Wang, W.,Chen, J.,Zhang, K.,Gao, F.,Gao, B.,Zhang, S.,Dong, M.,Besenbacher, F.,Gong, W.,Zhang, M.,Sun, F.,Feng, W.
Structural Insights Into the Intrinsic Self-Assembly of Par-3 N-Terminal Domain.
Structure, 21:997-, 2013

PubMed Abstract: Par-3, the central organizer of the Par-3/Par-6/atypical protein kinase C complex, is a multimodular scaffold protein that is essential for cell polarity establishment and maintenance. The N-terminal domain (NTD) of Par-3 is capable of self-association to form filament-like structures, although the underlying mechanism is poorly understood. Here, we determined the crystal structure of Par-3 NTD and solved the filament structure by cryoelectron microscopy. We found that an intrinsic "front-to-back" interaction mode is important for Par-3 NTD self-association and that both the lateral and longitudinal packing within the filament are mediated by electrostatic interactions. Disruptions of the lateral or longitudinal packing significantly impaired Par-3 NTD self-association and thereby impacted the Par-3-mediated epithelial polarization. We finally demonstrated that a Par-3 NTD-like domain from histidine ammonia-lyase also harbors a similar self-association capacity. This work unequivocally provides the structural basis for Par-3 NTD self-association and characterizes one type of protein domain that can self-assemble via electrostatic interactions.

PubMed: 23643951
DOI: 10.1016/J.STR.2013.04.004

実験手法

ELECTRON MICROSCOPY (6.1 Å)