7wab | pdb_00007wab

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

spinqualitylabelsall models 7wab, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7wab is a 1 chain structure with sequence from Aspergillus niger. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, NAG, MAN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A. 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. Crystal structure and substrate recognition mechanism of the prolyl endoprotease PEP from Aspergillus niger.,Miyazono KI, Kubota K, Takahashi K, Tanokura M Biochem Biophys Res Commun. 2022 Feb 5;591:76-81. doi:, 10.1016/j.bbrc.2021.12.114. Epub 2022 Jan 1. PMID:34999257 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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