Computational design of a homotrimeric metalloprotein with a trisbipyridyl core

Journal Article · 08 December 2016 · Proceedings of the National Academy of Sciences of the United States of America

DOI: https://doi.org/10.1073/pnas.1600188113 · OSTI ID:1335049

Mills, Jeremy H. ^[1]; Sheffler, William ^[2]; Ener, Maraia E. ^[3]; Almhjell, Patrick J. ^[4]; Oberdorfer, Gustav ^[2]; Pereira, José Henrique ^[5]; Parmeggiani, Fabio ^[2]; Sankaran, Banumathi ^[6]; Zwart, Peter H. ^[6]; Baker, David ^[7]

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1. Department of Biochemistry and the Institute for Protein Design, University of Washington, Seattle, WA 98195,, School of Molecular Sciences, Arizona State University, Tempe, AZ 85281,, The Biodesign Center for Molecular Design and Biomimetics, Arizona State University, Tempe, AZ 85281,
2. Department of Biochemistry and the Institute for Protein Design, University of Washington, Seattle, WA 98195,
3. Department of Biochemistry and the Institute for Protein Design, University of Washington, Seattle, WA 98195,, Department of Chemistry, University of Washington, Seattle, WA 98195,
4. School of Molecular Sciences, Arizona State University, Tempe, AZ 85281,, The Biodesign Center for Molecular Design and Biomimetics, Arizona State University, Tempe, AZ 85281,
5. Joint BioEnergy Institute, Emeryville, CA 94608,
6. Molecular Biophysics and Integrated Bioimaging, Berkeley Center for Structural Biology, Lawrence Berkeley National Laboratory, Berkeley, CA 94720,
7. Department of Biochemistry and the Institute for Protein Design, University of Washington, Seattle, WA 98195,, Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195

Significance This article reports the computational design of a threefold symmetric, self-assembling protein homotrimer containing a highly stable noncanonical amino acid-mediated metal complex within the protein interface. To achieve this result, recently developed protein–protein interface design methods were extended to include a metal-chelating noncanonical amino acid containing a bipyridine functional group in the design process. Bipyridine metal complexes can give rise to photochemical properties that would be impossible to achieve with naturally occurring amino acids alone, suggesting that the methods reported here could be used to generate novel photoactive proteins.

• Research Organization: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
• Sponsoring Organization: National Institutes of Health (NIH); US Department of the Navy, Office of Naval Research (ONR); USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
• Grant/Contract Number: AC02-05CH11231
• OSTI ID: 1335049
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 52 Vol. 113; ISSN 0027-8424
• Publisher: Proceedings of the National Academy of SciencesCopyright Statement
• Country of Publication: United States
• Language: English