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-Structure paper
Title | Mechanism of Actin Filament Severing and Capping by Gelsolin. |
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Journal, issue, pages | bioRxiv, Year 2024 |
Publish date | Sep 23, 2024 |
Authors | Kyle R Barrie / Grzegorz Rebowski / Roberto Dominguez |
PubMed Abstract | Gelsolin is the prototypical member of a family of Ca -dependent F-actin severing and capping proteins. A structure of Ca -bound full-length gelsolin at the barbed end shows domains G1G6 and the ...Gelsolin is the prototypical member of a family of Ca -dependent F-actin severing and capping proteins. A structure of Ca -bound full-length gelsolin at the barbed end shows domains G1G6 and the inter-domain linkers wrapping around F-actin. Another structure shows domains G1G3, a fragment produced during apoptosis, 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. |
External links | bioRxiv / PubMed:39345426 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.53 - 3.63 Å |
Structure data | EMDB-43262: Consensus map of full-length gelsolin bound to the barbed end of F-actin EMDB-43263: Local refinement of G1-G3 and F-actin barbed end subunits B-0 and B-2 EMDB-43264: Local refinement of G4-G6 and F-actin barbed end subunit B-1 EMDB-43268: Local refinement of F-actin barbed end subunits B-3, B-4, and B-5 EMDB-43274, PDB-8viz: EMDB-43316, PDB-8vkh: |
Chemicals | ChemComp-ADP: ChemComp-CA: ChemComp-ATP: |
Source |
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Keywords | PROTEIN BINDING / cytoskeleton / actin / cell motility |