Computational design of a homotrimeric metalloprotein with a trisbipyridyl core
Abstract
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.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Dec 08, 2016
- Source ID
- 10.1073/pnas.1600188113
Entities
People
- Banumathi Sankaran
- David Baker
- Fabio Parmeggiani
- Gustav Oberdorfer
- Jeremy H. Mills
- Jose Henrique Pereira
- Maraia E. Ener
- Patrick J Almhjell
- Peter H. Zwart
- William Sheffler
Organizations
- Arizona State University
- Defense Threat Reduction Agency
- European Commission
- Joint BioEnergy Institute
- Lawrence Berkeley National Laboratory
- National Institute of General Medical Sciences
- Office of Basic Energy Sciences
- Office of Naval Research Global
- Swiss National Science Foundation
- University of Washington