PDBsum entry 4eah

Protein binding

PDB id: 4eah

Contents

Protein chains

356 a.a.

357 a.a.

Ligands

ACT ×12

ATP ×4

PDB id:

4eah

Name:

Protein binding

Title:

Crystal structure of the formin homology 2 domain of fmnl3 bound to actin

Structure:

Actin, alpha skeletal muscle. Chain: d, h, g, f. Synonym: alpha-actin-1. Formin-like protein 3. Chain: a, e, c, b. Fragment: fh2 domain. Engineered: yes

Source:

Oryctolagus cuniculus. European rabbit,japanese white rabbit,domestic rabbit,rabbits. Organism_taxid: 9986. Mus musculus. Mouse. Organism_taxid: 10090. Gene: fmnl3, kiaa2014. Expressed in: escherichia coli.

Resolution:

3.40Å R-factor: 0.233 R-free: 0.277

Authors:

M.E.Thompson,E.G.Heimsath,T.J.Gauvin,H.N.Higgs,F.J.Kull

Key ref:

M.E.Thompson et al. (2013). FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation. Nat Struct Biol, 20, 111-118. PubMed id: 23222643

Date:

22-Mar-12 Release date: 12-Dec-12

Protein chains

P68135  (ACTS_RABIT) -  Actin, alpha skeletal muscle from Oryctolagus cuniculus

Seq: 377 a.a.

Struc: 356 a.a.

Protein chains

Q6ZPF4  (FMNL3_MOUSE) -  Formin-like protein 3 from Mus musculus

Seq: 1028 a.a.

Struc: 357 a.a.

Enzyme reactions

• Enzyme class 2: Chains A, E, C, B: E.C.?
• Enzyme class 3: Chains D, H, G, F: E.C.3.6.4.- - ?????

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Nat Struct Biol 20:111-118 (2013)

PubMed id: 23222643

FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation.

M.E.Thompson, E.G.Heimsath, T.J.Gauvin, H.N.Higgs, F.J.Kull.

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.