8VKH

Structure of gelsolin domains G1G3 bound to the barbed end of F-actin

Summary for 8VKH

Entry DOI	10.2210/pdb8vkh/pdb
Related	8VIZ
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	8
Total formula weight	419751.02
Authors	Barrie, K.R.,Rebowski, G.,Dominguez, R. (deposition date: 2024-01-09, release date: 2024-10-16, Last modification date: 2025-05-21)
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 Cited by 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 PDB entries with the same primary citation
Experimental method	ELECTRON MICROSCOPY (3.63 Å)

Structure validation