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6A4R

Crystal structure of aspartate bound peptidase E from Salmonella enterica

Summary for 6A4R
Entry DOI10.2210/pdb6a4r/pdb
Related1FY2
DescriptorPeptidase E, ASPARTIC ACID (3 entities in total)
Functional Keywordss51 peptidase, peptidase e, dimer, active site, active site loop, hydrolase
Biological sourceSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Total number of polymer chains2
Total formula weight57458.65
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 citationYadav, 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: 30194851
DOI: 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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