Watching the Evolution of a Protein’s Function
December 9, 2012
A major challenge in research to enable large-scale biofuels production is developing enzymes that are highly efficient in converting biomass components into usable fuels. Using directed evolution (i.e., a technique for modifying protein function), researchers have determined the structural basis for converting a noncatalytic small protein into an effective enzyme for for linking RNA molecules. Extended x-ray absorption fine structure (EXAFS) was used to determine the Zn-containing active-site structure of this RNA ligase, synthesized through in-vitro directed evolution.
F.-A. Chao, A. Morelli, J. C. Haugner, III, L. Churchfield, L. N. Hagmann, L. Shi, L. R. Masterson, R. Sarangi, G. Veglia and B. Seeling, “Structure and Dynamics of a Primordil Catalytic Fold Generated by in vitro Evolution”, Nat. Chem. Biol. 9, 81 (2013) doi: 10.1038/nchembio.1138
Funding Acknowledgements: Work supported by U.S. National Aeronautics and Space Administration (NASA) Agreement no. NNX09AH70A, through the NASA Astrobiology Institute–Ames Research Center (to F.-A.C., A.M., L.C. and B.S.); Minnesota Medical Foundation (to B.S.), and U.S. National Institutes of Health (NIH; T32 GM08347 to J.C.H., T32 DE007288 to L.R.M., GM100310 to G.V., and P41 RR001209). Stanford Synchrotron Radiation Lightsource (SSRL) at SLAC National Accelerator Laboratory (SLAC) operations funded by the Office of Basic Energy Sciences (OBES), U.S. Department of Energy (DOE) Office of Science. SSRL Structural Molecular Biology program supported by NIH National Center for Research Resources (NCRR) and Office of Biological Environmental Research (OBER), DOE Office of Science.