1. Structure of Asp‐bound peptidase E from Salmonella enterica: Active site at dimer interface illuminates Asp recognition.
- Author
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Yadav, Pooja, Goyal, Venuka Durani, Gaur, Neeraj K., Kumar, Ashwani, Gokhale, Sadashiv M., and Makde, Ravindra D.
- Subjects
PEPTIDASE ,SALMONELLA enterica ,TRANSPEPTIDATION ,DIPEPTIDES ,ASPARTIC acid ,ELECTROSTATICS - 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. The aspartate‐bound crystal structure of a peptidase E at 1.83 Å resolutionThe enzyme is a dimer, not a monomer, and the active site is shielded by dimer organizationThe previously unexplained Arg174 interacts with the active site upon dimerizationThe stringent aspartate specificity is due to electrostatics and tight packing. [ABSTRACT FROM AUTHOR]
- Published
- 2018
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