Martha L. Ludwig and Rowena G. Matthews are in the Department of Biological Chemistry and Biophysics Research Division, University of Michigan, 930 North University Avenue, Ann Arbor, Michigan 48109-1055, USA.
Correspondence should be addressed to Martha L. Ludwig mlludwig@umich.edu
The monomeric B12-dependent ribonucleotide reductase from L. leichmannii has the central 10-stranded /-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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-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.
