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1: Nat Chem Biol. 2008 Feb;4(2):107-9. Epub 2007 Dec 23.
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Cu(I) recognition via cation-pi and methionine interactions in CusF.

Xue Y, Davis AV, Balakrishnan G, Stasser JP, Staehlin BM, Focia P, Spiro TG, Penner-Hahn JE, O'Halloran TV.

Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, USA.

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.

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PMID: 18157124 [PubMed - indexed for MEDLINE]