7NIM
X-ray crystal structure of LsAA9A - cinnamon extract soak
Summary for 7NIM
| Entry DOI | 10.2210/pdb7nim/pdb |
| Related | 5ACH 5ACI |
| Descriptor | Auxiliary activity 9, COPPER (II) ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
| Functional Keywords | enzyme, complex, inhibitor, oxidoreductase |
| Biological source | Lentinus similis |
| Total number of polymer chains | 1 |
| Total formula weight | 27489.99 |
| Authors | Frandsen, K.E.H.,Tokin, R.,Skov, L.,Johansen, K.S.,Lo Leggio, L. (deposition date: 2021-02-12, release date: 2021-08-18, Last modification date: 2024-01-31) |
| Primary citation | Tokin, R.,Frandsen, K.E.H.,Ipsen, J.O.,Lo Leggio, L.,Poojary, M.M.,Berrin, J.G.,Grisel, S.,Brander, S.,Jensen, P.E.,Johansen, K.S. Inhibition of lytic polysaccharide monooxygenase by natural plant extracts. New Phytol., 232:1337-1349, 2021 Cited by PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes of industrial and biological importance. In particular, LPMOs play important roles in fungal lifestyle. No inhibitors of LPMOs have yet been reported. In this study, a diverse library of 100 plant extracts was screened for LPMO activity-modulating effects. By employing protein crystallography and LC-MS, we successfully identified a natural LPMO inhibitor. Extract screening revealed a significant LPMO inhibition by methanolic extract of Cinnamomum cassia (cinnamon), which inhibited LsAA9A LPMO from Lentinus similis in a concentration-dependent manner. With a notable exception, other microbial LPMOs from families AA9 and AA10 were also inhibited by this cinnamon extract. The polyphenol cinnamtannin B1 was identified as the inhibitory component by crystallography. Cinnamtannin B1 was bound to the surface of LsAA9A at two distinct binding sites: one close to the active site and another at a pocket on the opposite side of the protein. Independent characterization of cinnamon extract by LC-MS and subsequent activity measurements confirmed that the compound inhibiting LsAA9A was cinnamtannin B1. The results of this study show that specific natural LPMO inhibitors of plant origin exist in nature, providing the opportunity for future exploitation of such compounds within various biotechnological contexts. PubMed: 34389999DOI: 10.1111/nph.17676 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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