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Structure of Asp‐bound peptidase E from Salmonella enterica : Active site at dimer interface illuminates Asp recognition
Author(s) -
Yadav Pooja,
Goyal Venuka Durani,
Gaur Neeraj K.,
Kumar Ashwani,
Gokhale Sadashiv M.,
Makde Ravindra D.
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13247
Subject(s) - active site , dimer , chemistry , serine , enzyme , biochemistry , stereochemistry , biophysics , biology , organic chemistry
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.