1LQ7
De Novo Designed Protein Model of Radical Enzymes
Summary for 1LQ7
| Entry DOI | 10.2210/pdb1lq7/pdb |
| NMR Information | BMRB: 5356 |
| Descriptor | Alpha3W (1 entity in total) |
| Functional Keywords | three helix bundle, de novo protein |
| Total number of polymer chains | 1 |
| Total formula weight | 7562.90 |
| Authors | Dai, Q.-H.,Tommos, C.,Fuentes, E.J.,Blomberg, M.,Dutton, P.L.,Wand, A.J. (deposition date: 2002-05-09, release date: 2002-06-05, Last modification date: 2024-05-22) |
| Primary citation | Dai, Q.-H.,Tommos, C.,Fuentes, E.J.,Blomberg, M.,Dutton, P.L.,Wand, A.J. Structure of a De Novo Designed Protein Model of Radical Enzymes J.Am.Chem.Soc., 124:10952-10953, 2002 Cited by PubMed Abstract: The use of side chains as catalytic cofactors for protein mediated redox chemistry raises significant mechanistic issues as to how these amino acids are activated toward radical chemistry in a controlled manner. De novo protein design has been used to examine the structural basis for the creation and maintenance of a tryptophanyl radical in a three-helix bundle protein maquette. Here we report the detailed structural analysis of the protein by multidimensional NMR methods. An interesting feature of the structure is an apparent pi-cation interaction involving the sole tryptophan and a lysine side chain. Hybrid density functional calculations support the notion that this interaction raises the reduction potential of the W degrees /WH redox pair and helps explain the redox characteristics of the protein. This model protein system therefore provides a powerful model for exploring the structural basis for controlled radical chemistry in protein. PubMed: 12224922DOI: 10.1021/ja0264201 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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