9JW0

Structure of the N-terminal 3 domains (V1-V3) villin bound to actin

Summary for 9JW0

• Entry DOI: 10.2210/pdb9jw0/pdb
• Related: 9JUS 9JVT
• Descriptor: Villin, Actin, alpha skeletal muscle, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: villin actin, structural protein
• Biological source: Paralvinella sulfincola; More
• Total number of polymer chains: 2
• Total formula weight: 88047.29

Authors

Robinson, R.C. (deposition date: 2024-10-09, release date: 2025-10-15, Last modification date: 2025-12-17)

Primary citation

Robinson, R.C.,Chongrungreang, T.,Ponlachantra, K.,Boonyarit, B.,Dilly, G.F.,Li, Y.I.,Girguis, P.R.,Copley, R.R.,Claridge-Chang, A.
The structure of an actin nucleus stabilized by villin.
Sci Adv, 11:eadw6915-eadw6915, 2025

PubMed Abstract: Villin is an actin filament nucleating, severing, capping and bundling protein; however, the structural basis for villin's functions and the characteristics of the actin polymerization nucleus remain poorly understood. Here, we present the structure of vent-worm villin bound to a trimeric actin nucleus. Villin wraps around and caps the barbed end of the actin trimer. Its headpiece domain interacts at the junction of two laterally associated actin protomers, leaving the pointed-end subunits open for elongation. Within the actin trimer, the two longitudinally associated subunits adopt barbed and pointed-end subunit conformations, while the lateral protomer exhibits a monomeric conformation. This provides the first view of an actin-filament nucleus, revealing that the transition into the filamentous form is stimulated and stabilized by the interactions with the pointed-end subunits. Our results also illuminate mechanisms of actin-filament dynamics and villin capping and severing, suggesting that F-to-G actin conformational transitions facilitate the later process.

PubMed: 41337577
DOI: 10.1126/sciadv.adw6915

Experimental method

X-RAY DIFFRACTION (2.69 Å)