9RCL
Laccase (multicopper oxidase) from Pediococcus pentosaceus 4618 mutant M455A-M456A soaked with Copper 10 minutes
Summary for 9RCL
| Entry DOI | 10.2210/pdb9rcl/pdb |
| Related | 9RCJ 9RCK |
| Descriptor | Multicopper oxidase domain-containing protein, SULFATE ION, COPPER (II) ION, ... (4 entities in total) |
| Functional Keywords | laccase, oxidoreductase, multicopper oxidase |
| Biological source | Pediococcus pentosaceus 4618 |
| Total number of polymer chains | 3 |
| Total formula weight | 180821.03 |
| Authors | Paredes, F.,Casino, P. (deposition date: 2025-05-29, release date: 2025-11-19, Last modification date: 2026-01-14) |
| Primary citation | Gasco, R.,Sendra, R.,Olmeda, I.,Paredes-Martinez, F.,Ferrer, S.,Pardo, I.,Casino, P. Laccases from lactic acid bacteria show cuprous oxidase activity and capture Cu(II) and Ag(I) ions. Protein Sci., 35:e70385-e70385, 2026 Cited by PubMed Abstract: Several laccases derived from lactic acid bacteria (LAB) display specific structural features, such as two methionine residues at the entrance of the T1Cu center, and an extended C-terminal end enriched in methionine and histidine. To investigate their functional roles, we engineered mutant variants of the laccase Pp4816 from Pediococcus pentosaceus and analyzed them using both functional and structural approaches. We identified a cuprous oxidase activity that is essential for the oxidation of 2,6-dimethoxyphenol (2,6-DMP) and other substrates, but dispensable for ABTS. The two Met residues at the entrance of the T1Cu center are crucial for this activity while the C-terminus has a minor impact and shows conformational flexibility. Through anomalous diffraction studies, we located Cu(II) bound at the entrance of the T1Cu center and additional surface sites, and demonstrated that Ag(I) acts as an inhibitor of the cuprous oxidase activity, which binds to overlapping positions, including the C-terminus. This cuprous oxidase activity was found to be conserved in other laccases from LAB, suggesting that these enzymes function as copper and silver chelators with potential biotechnological applications, such as environmental copper detoxification. PubMed: 41432273DOI: 10.1002/pro.70385 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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