6A4R
Crystal structure of aspartate bound peptidase E from Salmonella enterica
Summary for 6A4R
Entry DOI | 10.2210/pdb6a4r/pdb |
Related | 1FY2 |
Descriptor | Peptidase E, ASPARTIC ACID (3 entities in total) |
Functional Keywords | s51 peptidase, peptidase e, dimer, active site, active site loop, hydrolase |
Biological source | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
Total number of polymer chains | 2 |
Total formula weight | 57458.65 |
Authors | Yadav, P.,Chandravanshi, K.,Goyal, V.D.,Singh, R.,Kumar, A.,Gokhale, S.M.,Makde, R.D. (deposition date: 2018-06-20, release date: 2018-10-24, Last modification date: 2023-11-22) |
Primary citation | Yadav, P.,Goyal, V.D.,Gaur, N.K.,Kumar, A.,Gokhale, S.M.,Makde, R.D. Structure of Asp-bound peptidase E from Salmonella enterica: Active site at dimer interface illuminates Asp recognition. FEBS Lett., 592:3346-3354, 2018 Cited by PubMed 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. PubMed: 30194851DOI: 10.1002/1873-3468.13247 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.828 Å) |
Structure validation
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