Structural Genomics of M. Jannaschii
One of the important objectives of decoding a genome (as in the Human Genome Project) is to understand the functions of all the gene products--mostly proteins. While the DNA sequence defines the series of linked amino acids that forms a protein, it is the folding of the protein that controls its function. Researchers in structural genomics use protein crystallography to determine the three-dimensional structures of proteins with an eye toward understanding protein function. To test the feasibility of this approach, researchers from UC Berkeley and Berkeley Lab are using the Macromolecular Crystallography Facility (MCF) at the ALS to study the fully sequenced bacterium Methanococcus jannaschii. Early results have already allowed the roles of two proteins to be tentatively identified from their structure alone.
Structure of hypothetical protein MJ0577. An electron-density map (left) derived from multiple-wavelength anomalous diffraction experiments clearly shows a bound ATP (yellow stick structure). The tertiary structure of MJ0577 (right) is a nucleotide binding fold. The discovery of the ATP immediately narrowed down the possible biochemical function of this protein. Subsequent biochemical assays indicated that it functions as a molecular switch for chemical reactions.
Research conducted by T. Zarembinski, L.-W. Hung, J. Mueller-Dieckmann, K.-K. Kim, H. Yokota, R. Kim, and S.-H. Kim (all of Berkeley Lab and University of California, Berkeley), using Beamline 5.0.2.
Funding: U. S. Department of Energy, Office of Biological and Environmental Research; Deutsche Forshungsgemeinshaft.
Publication about this experiment: T. Zarembinski, L.-W. Hung, J. Mueller-Dieckmann, K.-K. Kim, H. Yokota, R. Kim, and S.-H. Kim, Proc. Natl. Acad. Sci. 15 (1998), 15189.
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