Ontology highlight
ABSTRACT:
SUBMITTER: Pagba CV
PROVIDER: S-EPMC4686667 | biostudies-literature | 2015 Dec
REPOSITORIES: biostudies-literature
Nature communications 20151202
In class 1a ribonucleotide reductase (RNR), a substrate-based radical is generated in the α2 subunit by long-distance electron transfer involving an essential tyrosyl radical (Y122O·) in the β2 subunit. The conserved W48 β2 is ∼10 Å from Y122OH; mutations at W48 inactivate RNR. Here, we design a beta hairpin peptide, which contains such an interacting tyrosine-tryptophan dyad. The NMR structure of the peptide establishes that there is no direct hydrogen bond between the phenol and the indole rin ...[more]