Cu(I) recognition via cation-pi and methionine interactions in CusF.

ABSTRACT: Methionine-rich motifs have an important role in copper trafficking factors, including the CusF protein. Here we show that CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan. Spectroscopic studies demonstrate that both thioether ligation and strong cation-pi interactions with tryptophan stabilize metal binding. This novel active site chemistry affords mechanisms for control of adventitious metal redox and substitution chemistry.

SUBMITTER: Xue Y 

PROVIDER: S-EPMC2850561 | biostudies-literature |

REPOSITORIES: biostudies-literature