A Genetically Encoded Bidentate, Metal-Binding Amino Acid

Authors

  • Jianming Xie,

    1. Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd, La Jolla, CA 92037, USA, Fax: (+1) 858-784-9440
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  • Wenshe Liu Dr.,

    1. Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd, La Jolla, CA 92037, USA, Fax: (+1) 858-784-9440
    2. Current address: Department of Chemistry, Texas A&M University, College Station, TX 77843
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  • Peter G. Schultz Prof. Dr.

    1. Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd, La Jolla, CA 92037, USA, Fax: (+1) 858-784-9440
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  • We thank Dr. Lubica Supekova, Chang Liu, Eric Brustad, Hyunsoo Lee, and Emily Remba for experimental assistance and helpful discussions. This work is supported by a grant from the Department of Energy ER46051 and the Skaggs Institute for Chemical Biology.

Abstract

original image

A two-ring binder: To facilitate the design of metalloproteins, the bidentate, metal-binding amino acid bipyridylalanine (BpyAla) was genetically encoded in E. coli in response to the amber nonsense codon with high fidelity and yield. The incorporation of BpyAla requires a BpyAla-specific aminoacyl-tRNA synthetase, which was evolved in a stepwise fashion. The structural basis of selective recognition of BpyAla by this synthetase was also determined.

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