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-pi 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

Top

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.

Top
  1. Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, USA.
  2. Department of Chemistry, University of Washington, Box 351700, Seattle, Washington 98195, USA.
  3. Department of Chemistry and Biophysics Program, University of Michigan, 930 North University Avenue, Ann Arbor, Michigan 48109, USA.
  4. Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Medical School, 303 East Chicago Avenue, Chicago, Illinois 60611, USA.
  5. Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2205 Tech Drive, Evanston, Illinois 60208, USA.
  6. These authors contributed equally to this work.

Correspondence to: Thomas V O'Halloran1,5 e-mail: t-ohalloran@northwestern.edu



MORE ARTICLES LIKE THIS

These links to content published by NPG are automatically generated.

NEWS AND VIEWS

Copper shares a piece of the π

Nature Chemical Biology News and Views (01 Feb 2008)

Neuropharmacology of peptides

Nature News and Views (20 Dec 1974)