4RWT

Structure of actin-Lmod complex

4RWT の概要

• エントリーDOI: 10.2210/pdb4rwt/pdb
• 分子名称: Actin-5C, Leiomodin-2, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: leucine rich region, actin nucleation, actin, structural protein
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P10987
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 200341.99

構造登録者

Chen, X.,Ni, F.,Wang, Q. (登録日: 2014-12-05, 公開日: 2015-10-14, 最終更新日: 2024-02-28)

主引用文献

Chen, X.,Ni, F.,Kondrashkina, E.,Ma, J.,Wang, Q.
Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells.
Proc.Natl.Acad.Sci.USA, 112:12687-12692, 2015

PubMed Abstract: Leiomodin (Lmod) is a class of potent tandem-G-actin-binding nucleators in muscle cells. Lmod mutations, deletion, or instability are linked to lethal nemaline myopathy. However, the lack of high-resolution structures of Lmod nucleators in action severely hampered our understanding of their essential cellular functions. Here we report the crystal structure of the actin-Lmod2162-495 nucleus. The structure contains two actin subunits connected by one Lmod2162-495 molecule in a non-filament-like conformation. Complementary functional studies suggest that the binding of Lmod2 stimulates ATP hydrolysis and accelerates actin nucleation and polymerization. The high level of conservation among Lmod proteins in sequence and functions suggests that the mechanistic insights of human Lmod2 uncovered here may aid in a molecular understanding of other Lmod proteins. Furthermore, our structural and mechanistic studies unraveled a previously unrecognized level of regulation in mammalian signal transduction mediated by certain tandem-G-actin-binding nucleators.

PubMed: 26417072
DOI: 10.1073/pnas.1512464112

実験手法

X-RAY DIFFRACTION (2.98 Å)