Dataset for: Structure of Asp-bound Peptidase E from Salmonella enterica: Active site at dimer interface illuminates Asp recognition

Peptidase-E, a non-classical serine peptidase, is specific for dipeptides with N-terminal aspartate. This stringent substrate specificity remains largely unexplained. We report an aspartate-bound structure of Peptidase-E at 1.83 Å resolution. In contrast to previous reports, the enzyme forms a dimer and the active site is located at dimer interface, well shielded from the solvent. Role of functionally important residues can now be explained on the basis of new structural information. Stringent aspartate specificity of the enzyme is due to electrostatics and molecular complementarity in the active site.