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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 | 2008 Feb

REPOSITORIES: biostudies-literature

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

Xue Yi Y Davis Anna V AV Balakrishnan Gurusamy G Stasser Jay P JP Staehlin Benjamin M BM Focia Pamela P Spiro Thomas G TG Penner-Hahn James E JE O'Halloran Thomas V TV

Nature chemical biology 20071223 2

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 subst ...[more]

PMID: 18157124

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