6NFF

Structure of X-prolyl dipeptidyl aminopeptidase from Lactobacillus helveticus

6NFF の概要

• エントリーDOI: 10.2210/pdb6nff/pdb
• 分子名称: Xaa-Pro dipeptidyl-peptidase, CALCIUM ION, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, peptidase
• 由来する生物種: Lactobacillus helveticus (Lactobacillus suntoryeus)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 94117.01

構造登録者

Juers, D.H.,Bratt, N.J.,Ojennus, D.D. (登録日: 2018-12-20, 公開日: 2019-10-02, 最終更新日: 2023-10-11)

主引用文献

Ojennus, D.D.,Bratt, N.J.,Jones, K.L.,Juers, D.H.
Structural characterization of a prolyl aminodipeptidase (PepX) from Lactobacillus helveticus.
Acta Crystallogr.,Sect.F, 75:625-633, 2019

PubMed Abstract: Prolyl aminodipeptidase (PepX) is an enzyme that hydrolyzes peptide bonds from the N-terminus of substrates when the penultimate amino-acid residue is a proline. Prolyl peptidases are of particular interest owing to their ability to hydrolyze food allergens that contain a high percentage of proline residues. PepX from Lactobacillus helveticus was cloned and expressed in Escherichia coli as an N-terminally His-tagged recombinant construct and was crystallized by hanging-drop vapor diffusion in a phosphate buffer using PEG 3350 as a precipitant. The structure was determined at 2.0 Å resolution by molecular replacement using the structure of PepX from Lactococcus lactis (PDB entry 1lns) as the starting model. Notable differences between the L. helveticus PepX structure and PDB entry 1lns include a cysteine instead of a phenylalanine at the substrate-binding site in the position which confers exopeptidase activity and the presence of a calcium ion coordinated by a calcium-binding motif with the consensus sequence DX(DN)XDG.

PubMed: 31584010
DOI: 10.1107/S2053230X19011774

実験手法

X-RAY DIFFRACTION (2 Å)