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Effector regulation in a monomeric enzyme

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The monomeric B12-dependent ribonucleotide reductase from L. leichmannii has the central 10-stranded α/β-barrel found in all ribonucleotide reductases but incorporates two distinctive structural features, a novel cobalamin-binding fold and an insert forming part of a specificity control site that mimics the allosteric site found in the oligomeric di-iron dependent reductases.

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Figure 1: Formation of the thiyl radical in class II ribonucleotide reductases.
Figure 2: Arrangement of the players in the reduction of ribonucleotides.

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Authors and Affiliations

  1. the Department of Biological Chemistry and Biophysics Research Division, University of Michigan, 930 North University Avenue, Ann Arbor, 48109-1055, Michigan, USA

    Martha L. Ludwig & Rowena G. Matthews

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  1. Martha L. Ludwig
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  2. Rowena G. Matthews
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Correspondence to Martha L. Ludwig.

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Ludwig, M., Matthews, R. Effector regulation in a monomeric enzyme. Nat Struct Mol Biol 9, 236–238 (2002). https://doi.org/10.1038/nsb0402-236

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