Structural highlights
Function
PEPE_SALTY Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.[HAMAP-Rule:MF_00510]
Publication Abstract from PubMed
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 A 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.
Structure of Asp-bound peptidase E from Salmonella enterica: Active site at dimer interface illuminates Asp recognition.,Yadav P, Goyal VD, Gaur NK, Kumar A, Gokhale SM, Makde RD FEBS Lett. 2018 Oct;592(19):3346-3354. doi: 10.1002/1873-3468.13247. Epub 2018, Sep 21. PMID:30194851[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yadav P, Goyal VD, Gaur NK, Kumar A, Gokhale SM, Makde RD. Structure of Asp-bound peptidase E from Salmonella enterica: Active site at dimer interface illuminates Asp recognition. FEBS Lett. 2018 Oct;592(19):3346-3354. doi: 10.1002/1873-3468.13247. Epub 2018, Sep 21. PMID:30194851 doi:http://dx.doi.org/10.1002/1873-3468.13247
