4A68
Mutations in the neighbourhood of CotA-laccase trinuclear site: D116N mutant
Summary for 4A68
| Entry DOI | 10.2210/pdb4a68/pdb |
| Related | 1GSK 1OF0 1UVW 1W6L 1W6W 1W8E 2BHF 2X87 2X88 4A66 4A67 |
| Descriptor | SPORE COAT PROTEIN A, COPPER (II) ION, HYDROXIDE ION, ... (7 entities in total) |
| Functional Keywords | oxidoreductase, multi-copper oxidase, oxidoreductase activity, trinuclear cluster, dioxygen reduction |
| Biological source | BACILLUS SUBTILIS |
| Total number of polymer chains | 1 |
| Total formula weight | 59351.65 |
| Authors | Silva, C.S.,Lindley, P.F.,Bento, I. (deposition date: 2011-10-31, release date: 2012-01-25, Last modification date: 2024-11-06) |
| Primary citation | Silva, C.S.,Damas, J.M.,Chen, Z.,Brissos, V.,Martins, L.O.,Soares, C.M.,Lindley, P.F.,Bento, I. The Role of Asp116 in the Reductive Cleavage of Dioxygen to Water in Cota Laccase: Assistance During the Proton Transfer Mechanism Acta Crystallogr.,Sect.D, 68:186-, 2012 Cited by PubMed Abstract: Multi-copper oxidases constitute a family of proteins that are capable of coupling the one-electron oxidation of four substrate equivalents to the four-electron reduction of dioxygen to two molecules of water. The main catalytic stages occurring during the process have already been identified, but several questions remain, including the nature of the protonation events that take place during the reductive cleavage of dioxygen to water. The presence of a structurally conserved acidic residue (Glu498 in CotA laccase from Bacillus subtilis) at the dioxygen-entrance channel has been reported to play a decisive role in the protonation mechanisms, channelling protons during the reduction process and stabilizing the site as a whole. A second acidic residue that is sequentially conserved in multi-copper oxidases and sited within the exit channel (Asp116 in CotA) has also been identified as being important in the protonation process. In this study, CotA laccase has been used as a model system to assess the role of Asp116 in the reduction process of dioxygen to water. The crystal structures of three distinct mutants, D116E, D116N and D116A, produced by site-saturation mutagenesis have been determined. In addition, theoretical calculations have provided further support for a role of this residue in the protonation events. PubMed: 22281748DOI: 10.1107/S0907444911054503 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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