8VIZ

Structure of full-length gelsolin bound to the barbed end of F-actin

Summary for 8VIZ

• Entry DOI: 10.2210/pdb8viz/pdb
• Related: 8VKH
• EMDB information: 43274 43316
• Descriptor: Actin, alpha skeletal muscle, Gelsolin, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: cytoskeleton, actin, cell motility, protein binding
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 7
• Total formula weight: 337195.76

Authors

Barrie, K.R.,Rebowski, G.,Dominguez, R. (deposition date: 2024-01-05, release date: 2024-10-16, Last modification date: 2025-06-04)

Primary citation

Barrie, K.R.,Rebowski, G.,Dominguez, R.
Mechanism of actin filament severing and capping by gelsolin.
Nat.Struct.Mol.Biol., 32:237-242, 2025

PubMed Abstract: Gelsolin is the prototypical member of a family of Ca-activated F-actin severing and capping proteins. Here we report structures of Ca-bound human gelsolin at the barbed end of F-actin. One structure reveals gelsolin's six domains (G1G6) and interdomain linkers wrapping around F-actin, while another shows domains G1G3-a fragment observed during apoptosis-binding on both sides of F-actin. Conformational changes that trigger severing occur on one side of F-actin with G1G6 and on both sides with G1G3. Gelsolin remains bound after severing, blocking subunit exchange.

PubMed: 39448849
DOI: 10.1038/s41594-024-01412-5

Experimental method

ELECTRON MICROSCOPY (2.63 Å)