4EAH

Crystal structure of the formin homology 2 domain of FMNL3 bound to actin

Summary for 4EAH

• Entry DOI: 10.2210/pdb4eah/pdb
• Descriptor: Actin, alpha skeletal muscle, Formin-like protein 3, ACETATE ION, ... (4 entities in total)
• Functional Keywords: atp binding, cytoskeleton, formin, fmnl3, actin, protein binding
• Biological source: Mus musculus (mouse); More
• Cellular location: Cytoplasm, cytoskeleton: P68135; Cytoplasm : Q6ZPF4
• Total number of polymer chains: 8
• Total formula weight: 355165.96

Authors

Thompson, M.E.,Heimsath, E.G.,Gauvin, T.J.,Higgs, H.N.,Kull, F.J. (deposition date: 2012-03-22, release date: 2012-12-12, Last modification date: 2024-02-28)

Primary citation

Thompson, M.E.,Heimsath, E.G.,Gauvin, T.J.,Higgs, H.N.,Kull, F.J.
FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation.
Nat.Struct.Mol.Biol., 20:111-118, 2013

PubMed Abstract: Formins are actin-assembly factors that act in a variety of actin-based processes. The conserved formin homology 2 (FH2) domain promotes filament nucleation and influences elongation through interaction with the barbed end. FMNL3 is a formin that induces assembly of filopodia but whose FH2 domain is a poor nucleator. The 3.4-Å structure of a mouse FMNL3 FH2 dimer in complex with tetramethylrhodamine-actin uncovers details of formin-regulated actin elongation. We observe distinct FH2 actin-binding regions; interactions in the knob and coiled-coil subdomains are necessary for actin binding, whereas those in the lasso-post interface are important for the stepping mechanism. Biochemical and cellular experiments test the importance of individual residues for function. This structure provides details for FH2-mediated filament elongation by processive capping and supports a model in which C-terminal non-FH2 residues of FMNL3 are required to stabilize the filament nucleus.

PubMed: 23222643
DOI: 10.1038/nsmb.2462

Experimental method

X-RAY DIFFRACTION (3.4 Å)