7WAB

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

Summary for 7WAB

• Entry DOI: 10.2210/pdb7wab/pdb
• Descriptor: 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)
• Functional Keywords: protease, hydrolase
• Biological source: Aspergillus niger
• Total number of polymer chains: 1
• Total formula weight: 56384.12

Authors

Miyazono, K.,Kubota, K.,Takahashi, K.,Tanokura, M. (deposition date: 2021-12-14, release date: 2022-01-12, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.75 Å)