5I9E

Crystal structure of a nuclear actin ternary complex

5I9E の概要

• エントリーDOI: 10.2210/pdb5i9e/pdb
• 分子名称: Actin-related protein 4, Actin, Helicase SWR1, ... (5 entities in total)
• 機能のキーワード: nuclear actin, arp4, chromatin remodeling, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 213015.35

構造登録者

Chen, Z.,Cao, T. (登録日: 2016-02-20, 公開日: 2016-07-27, 最終更新日: 2023-11-08)

主引用文献

Cao, T.,Sun, L.,Jiang, Y.,Huang, S.,Wang, J.,Chen, Z.
Crystal structure of a nuclear actin ternary complex.
Proc.Natl.Acad.Sci.USA, 113:8985-8990, 2016

PubMed Abstract: Actin polymerizes and forms filamentous structures (F-actin) in the cytoplasm of eukaryotic cells. It also exists in the nucleus and regulates various nucleic acid transactions, particularly through its incorporation into multiple chromatin-remodeling complexes. However, the specific structure of actin and the mechanisms that regulate its polymeric nature inside the nucleus remain unknown. Here, we report the crystal structure of nuclear actin (N-actin) complexed with actin-related protein 4 (Arp4) and the helicase-SANT-associated (HSA) domain of the chromatin remodeler Swr1. The inner face and barbed end of N-actin are sequestered by interactions with Arp4 and the HSA domain, respectively, which prevents N-actin from polymerization and binding to many actin regulators. The two major domains of N-actin are more twisted than those of globular actin (G-actin), and its nucleotide-binding pocket is occluded, freeing N-actin from binding to and regulation by ATP. These findings revealed the salient structural features of N-actin that distinguish it from its cytoplasmic counterpart and provide a rational basis for its functions and regulation inside the nucleus.

PubMed: 27457955
DOI: 10.1073/pnas.1602818113

実験手法

X-RAY DIFFRACTION (2.8 Å)