1. Cu(i) recognition via cation-π and methionine interactions in CusF
- Author
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Yi Xue, Jay Stasser, Pamela J. Focia, Thomas V. O'Halloran, James E. Penner-Hahn, Gurusamy Balakrishnan, Thomas G. Spiro, Benjamin M. Staehlin, and Anna V Davis
- Subjects
Models, Molecular ,Stereochemistry ,Redox ,Article ,Metal ,chemistry.chemical_compound ,Methionine ,Copper Transport Proteins ,Thioether ,Cations ,Cation Transport Proteins ,Molecular Biology ,Substitution reaction ,biology ,Ligand ,Escherichia coli Proteins ,Tryptophan ,Active site ,Cell Biology ,Protein Structure, Tertiary ,chemistry ,visual_art ,Biophysics ,biology.protein ,visual_art.visual_art_medium ,Copper ,Protein Binding - 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.
- Published
- 2007