Frédéric Kerff

TL;DR: An overview of the content in PBPs of some bacteria is provided with an emphasis on comparing the biochemical properties of homologous PBPs (orthologues) belonging to different bacteria.

TL;DR: Structural elements amino- and carboxy-terminal to the RVxF motif of MYPT1 are positioned in a way that leads to a pronounced reshaping of the catalytic cleft of PP1, contributing to the increased myosin specificity of this complex.

TL;DR: The crystal structures of complexes of actin with the WH2 domains of WASP, WasP-family verprolin homologous protein, and WASP-interacting protein are described and a mechanism for how profilin-binding Pro-rich sequences positioned N-terminal to WH2 could feed actin monomers directly to WH1, thereby playing a role in filament elongation is suggested.

TL;DR: The crystal structure of a secreted protein, EXLX1, encoded by the yoaJ gene of Bacillus subtilis, is solved and the discovery of a bacterial homolog opens the door for detailed structural studies of expansin function.

TL;DR: Comparison of the structures of MIM's IMD and that of its WH2 bound to actin reveals that the membrane binding surfaces of the two domains have opposite curvatures, which may determine the type of curvature of the interacting membrane.