4EAH

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


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.277 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.233 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

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

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

(2013) Nat Struct Mol Biol 20: 111-118

  • DOI: https://doi.org/10.1038/nsmb.2462
  • Primary Citation of Related Structures:  
    4EAH

  • 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.


  • Organizational Affiliation

    Department of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Actin, alpha skeletal muscleA [auth D],
F [auth H],
G,
H [auth F]
377Oryctolagus cuniculusMutation(s): 0 
UniProt
Find proteins for P68135 (Oryctolagus cuniculus)
Explore P68135 
Go to UniProtKB:  P68135
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP68135
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Formin-like protein 3B [auth A],
C [auth E],
D [auth C],
E [auth B]
402Mus musculusMutation(s): 0 
Gene Names: Fmnl3Kiaa2014
UniProt & NIH Common Fund Data Resources
Find proteins for Q6ZPF4 (Mus musculus)
Explore Q6ZPF4 
Go to UniProtKB:  Q6ZPF4
IMPC:  MGI:109569
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6ZPF4
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ATP
Query on ATP

Download Ideal Coordinates CCD File 
J [auth D],
S [auth H],
U [auth G],
X [auth F]
ADENOSINE-5'-TRIPHOSPHATE
C10 H16 N5 O13 P3
ZKHQWZAMYRWXGA-KQYNXXCUSA-N
ACT
Query on ACT

Download Ideal Coordinates CCD File 
I [auth D]
K [auth A]
L [auth A]
M [auth A]
N [auth E]
I [auth D],
K [auth A],
L [auth A],
M [auth A],
N [auth E],
O [auth C],
P [auth C],
Q [auth B],
R [auth H],
T [auth G],
V [auth F],
W [auth F]
ACETATE ION
C2 H3 O2
QTBSBXVTEAMEQO-UHFFFAOYSA-M
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.277 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.233 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 125.98α = 90
b = 126.05β = 93.17
c = 129.62γ = 90
Software Package:
Software NamePurpose
JBluIce-EPICSdata collection
PHENIXmodel building
PHENIXrefinement
XDSdata reduction
XDSdata scaling
PHENIXphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-12-12
    Type: Initial release
  • Version 1.1: 2012-12-26
    Changes: Database references
  • Version 1.2: 2013-01-16
    Changes: Database references
  • Version 1.3: 2017-11-15
    Changes: Advisory, Refinement description
  • Version 1.4: 2024-02-28
    Changes: Advisory, Data collection, Database references, Derived calculations