2FF3

Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin

Summary for 2FF3

• Entry DOI: 10.2210/pdb2ff3/pdb
• Descriptor: Gelsolin, Neural Wiskott-Aldrich syndrome protein, Actin, alpha skeletal muscle, ... (6 entities in total)
• Functional Keywords: protein-protein complex, structural protein-contractile protein complex, structural protein/contractile protein
• Biological source: Homo sapiens (human); More
• Cellular location: Isoform 2: Cytoplasm, cytoskeleton. Isoform 1: Secreted: P06396; Cytoplasm, cytoskeleton (By similarity): O00401; Cytoplasm, cytoskeleton: P68135
• Total number of polymer chains: 3
• Total formula weight: 60813.50

Authors

Xue, B.,Aguda, A.H.,Robinson, R.C. (deposition date: 2005-12-19, release date: 2006-03-21, Last modification date: 2024-10-09)

Primary citation

Aguda, A.H.,Xue, B.,Irobi, E.,Preat, T.,Robinson, R.C.
The Structural Basis of Actin Interaction with Multiple WH2/beta-Thymosin Motif-Containing Proteins
Structure, 14:469-476, 2006

PubMed Abstract: Participation of actin in cellular processes relies on the dynamics of filament assembly. Filament elongation is fed by monomeric actin in complex with either profilin or a Wiscott-Aldrich syndrome protein (WASP) homology domain 2 (WH2)/beta-thymosin (betaT) domain. WH2/betaT motif repetition (typified by ciboulot) or combination with nonrelated domains (as found in N-WASP) results in proteins that yield their actin to filament elongation. Here, we report the crystal structures of actin bound hybrid proteins, constructed between gelsolin and WH2/betaT domains from ciboulot or N-WASP. We observe the C-terminal half of ciboulot domain 2 bound to actin. In solution, we show that cibolout domains 2 and 3 bind to both G- and F-actin, and that whole ciboulot forms a complex with two actin monomers. In contrast, the analogous portion of N-WASP WH2 domain 2 is detached from actin, indicating that the C-terminal halves of the betaT and WH2 motifs are not functionally analogous.

PubMed: 16531231
DOI: 10.1016/j.str.2005.12.011

Experimental method

X-RAY DIFFRACTION (2 Å)