6A4R

Crystal structure of aspartate bound peptidase E from Salmonella enterica

6A4R の概要

• エントリーDOI: 10.2210/pdb6a4r/pdb
• 関連するPDBエントリー: 1FY2
• 分子名称: Peptidase E, ASPARTIC ACID (3 entities in total)
• 機能のキーワード: s51 peptidase, peptidase e, dimer, active site, active site loop, hydrolase
• 由来する生物種: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57458.65

構造登録者

Yadav, P.,Chandravanshi, K.,Goyal, V.D.,Singh, R.,Kumar, A.,Gokhale, S.M.,Makde, R.D. (登録日: 2018-06-20, 公開日: 2018-10-24, 最終更新日: 2023-11-22)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.828 Å)