The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins.
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.
Mesh Terms:
Actins, Amino Acid Sequence, Animals, Drosophila, Drosophila Proteins, Gelsolin, Microfilament Proteins, Models, Molecular, Molecular Sequence Data, Nerve Tissue Proteins, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Structure-Activity Relationship, Thymosin, Wiskott-Aldrich Syndrome Protein
Actins, Amino Acid Sequence, Animals, Drosophila, Drosophila Proteins, Gelsolin, Microfilament Proteins, Models, Molecular, Molecular Sequence Data, Nerve Tissue Proteins, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Structure-Activity Relationship, Thymosin, Wiskott-Aldrich Syndrome Protein
Structure
Date: Mar. 01, 2006
PubMed ID: 16531231
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