4RWT

Structure of actin-Lmod complex

Summary for 4RWT

• Entry DOI: 10.2210/pdb4rwt/pdb
• Descriptor: Actin-5C, Leiomodin-2, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• Functional Keywords: leucine rich region, actin nucleation, actin, structural protein
• Biological source: Drosophila melanogaster (Fruit fly); More
• Cellular location: Cytoplasm, cytoskeleton: P10987
• Total number of polymer chains: 4
• Total formula weight: 200341.99

Authors

Chen, X.,Ni, F.,Wang, Q. (deposition date: 2014-12-05, release date: 2015-10-14, Last modification date: 2024-02-28)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.98 Å)