1lq7 | pdb_00001lq7
De Novo Designed Protein Model of Radical Enzymes
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Overview
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.
About this Structure
1LQ7 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structure of a de novo designed protein model of radical enzymes., Dai QH, Tommos C, Fuentes EJ, Blomberg MR, Dutton PL, Wand AJ, J Am Chem Soc. 2002 Sep 18;124(37):10952-3. PMID:12224922 [[Category: ]]
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