| Structural highlights
9qr8 is a 1 chain structure with sequence from Nepenthes alata x Nepenthes ventricosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.9Å |
| Ligands: | BMA, CL, FUC, GLY, GOL, NAG, PEG, SO4, TRS |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
NEPRN_NEPVE Glutamic endopeptidase that preferentially cleaves peptide bonds on the C-terminal side of proline residues (PubMed:27481162, PubMed:28404794, PubMed:35915115). Also cleaves peptide bonds on the C-terminal side of alanine residues but with less efficiency (PubMed:28404794). In contrast to most proline-cleaving enzymes, effectively degrades proteins of any size (PubMed:28404794). Found in the viscoelastic fluid of the pitcher, and so likely functions in the digestion of their prey (PubMed:27481162).[1] [2] [3]
References
- ↑ Rey M, Yang M, Lee L, Zhang Y, Sheff JG, Sensen CW, Mrazek H, Halada P, Man P, McCarville JL, Verdu EF, Schriemer DC. Addressing proteolytic efficiency in enzymatic degradation therapy for celiac disease. Sci Rep. 2016 Aug 2;6:30980. PMID:27481162 doi:10.1038/srep30980
- ↑ Schräder CU, Lee L, Rey M, Sarpe V, Man P, Sharma S, Zabrouskov V, Larsen B, Schriemer DC. Neprosin, a Selective Prolyl Endoprotease for Bottom-up Proteomics and Histone Mapping. Mol Cell Proteomics. 2017 Jun;16(6):1162-1171. PMID:28404794 doi:10.1074/mcp.M116.066803
- ↑ Del Amo-Maestro L, Mendes SR, Rodríguez-Banqueri A, Garzon-Flores L, Girbal M, Rodríguez-Lagunas MJ, Guevara T, Franch À, Pérez-Cano FJ, Eckhard U, Gomis-Rüth FX. Molecular and in vivo studies of a glutamate-class prolyl-endopeptidase for coeliac disease therapy. Nat Commun. 2022 Aug 1;13(1):4446. PMID:35915115 doi:10.1038/s41467-022-32215-1
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