1. Structure of Asp-bound peptidase E from Salmonella enterica: Active site at dimer interface illuminates Asp recognition.
- Author
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Yadav P, Goyal VD, Gaur NK, Kumar A, Gokhale SM, and Makde RD
- Subjects
- Aminopeptidases metabolism, Aspartic Acid metabolism, Bacterial Proteins metabolism, Binding Sites, Catalytic Domain, Crystallography, X-Ray, Models, Molecular, Protein Conformation, Protein Multimerization, Salmonella enterica metabolism, Static Electricity, Aminopeptidases chemistry, Aspartic Acid chemistry, Bacterial Proteins chemistry, Salmonella enterica enzymology
- Abstract
Peptidase-E, a nonclassical serine peptidase, is specific for dipeptides with an 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 the dimer interface, well shielded from the solvent. Our findings further suggest that the stringent aspartate specificity of the enzyme is due to electrostatics and molecular complementarity in the active site. The new structural information presented herein may provide insights into the role of functionally important residues in peptidase-E., (© 2018 Federation of European Biochemical Societies.)
- Published
- 2018
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