Brief Communication abstract
Nature Chemical Biology 4, 107 - 109 (2007)
Published online: 23 December 2007 | doi:10.1038/nchembio.2007.57
Cu(I) recognition via cation-
and methionine interactions in CusF
Yi Xue1,6, Anna V Davis1,6, Gurusamy Balakrishnan2, Jay P Stasser3, Benjamin M Staehlin1, Pamela Focia4, Thomas G Spiro2, James E Penner-Hahn3 & Thomas V O'Halloran1,5
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-
interactions with tryptophan stabilize metal binding. This novel active site chemistry affords mechanisms for control of adventitious metal redox and substitution chemistry.
- Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, USA.
- Department of Chemistry, University of Washington, Box 351700, Seattle, Washington 98195, USA.
- Department of Chemistry and Biophysics Program, University of Michigan, 930 North University Avenue, Ann Arbor, Michigan 48109, USA.
- Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Medical School, 303 East Chicago Avenue, Chicago, Illinois 60611, USA.
- Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2205 Tech Drive, Evanston, Illinois 60208, USA.
- These authors contributed equally to this work.
Correspondence to: Thomas V O'Halloran1,5 e-mail: t-ohalloran@northwestern.edu
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