7WAB

Crystal structure of the prolyl endoprotease, PEP, from Aspergillus niger

7WAB の概要

• エントリーDOI: 10.2210/pdb7wab/pdb
• 分子名称: COMPASS (Complex proteins associated with Set1p) component shg1 family protein, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: protease, hydrolase
• 由来する生物種: Aspergillus niger
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56384.12

構造登録者

Miyazono, K.,Kubota, K.,Takahashi, K.,Tanokura, M. (登録日: 2021-12-14, 公開日: 2022-01-12, 最終更新日: 2024-11-13)

主引用文献

Miyazono, K.I.,Kubota, K.,Takahashi, K.,Tanokura, M.
Crystal structure and substrate recognition mechanism of the prolyl endoprotease PEP from Aspergillus niger.
Biochem.Biophys.Res.Commun., 591:76-81, 2022

PubMed Abstract: Proteases are enzymes that are not only essential for life but also industrially important. Understanding the substrate recognition mechanisms of proteases is important to enhance the use of proteases. The fungus Aspergillus produces a wide variety of proteases, including PEP, which is a prolyl endoprotease from A. niger. Although PEP exhibits amino acid sequence similarity to the serine peptidase family S28 proteins (PRCP and DPP7) that recognize Pro-X bonds in the terminal regions of peptides, PEP recognizes Pro-X bonds not only in peptides but also in proteins. To reveal the structural basis of the prolyl endoprotease activity of PEP, we determined the structure of PEP by X-ray crystallography at a resolution of 1.75 Å. The PEP structure shows that PEP has a wide-open catalytic pocket compared to its homologs. The characteristic catalytic pocket structure of PEP is predicted to be important for the recognition of protein substrates.

PubMed: 34999257
DOI: 10.1016/j.bbrc.2021.12.114

実験手法

X-RAY DIFFRACTION (1.75 Å)