Structure of the tropomyosin overlap complex from chicken smooth muscle: insight into the diversity of N-terminal recognition.

ABSTRACT: Tropomyosin is a stereotypical alpha-helical coiled coil that polymerizes to form a filamentous macromolecular assembly that lies on the surface of F-actin. The interaction between the C-terminal and N-terminal segments on adjacent molecules is known as the overlap region. We report here two X-ray structures of the chicken smooth muscle tropomyosin overlap complex. A novel approach was used to stabilize the C-terminal and N-terminal fragments. Globular domains from both the human DNA ligase binding protein XRCC4 and bacteriophage varphi29 scaffolding protein Gp7 were fused to 37 and 28 C-terminal amino acid residues of tropomyosin, respectively, whereas the 29 N-terminal amino acids of tropomyosin were fused to the C-terminal helix bundle of microtubule binding protein EB1. The structures

SUBMITTER: Frye J 

PROVIDER: S-EPMC2883815 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature