Faculté des sciences

## Crystallographic Analysis of a Full-length Streptavidin with Its C-terminal Polypeptide Bound in the Biotin Binding Site

### In: Journal of Molecular Biology, 2006, vol. 356, p. 738-745

The structure of a full-length streptavidin has been determined at 1.7 Å resolution and shows that the 20 residue extension at the C terminus forms a well-ordered polypeptide loop on the surface of the tetramer. Residues 150–153 of the extension are bound to the ligand-binding site, possibly competing with exogenous ligands. The binding mode of these residues is compared with that of biotin... More