Upton, NY--Two reports in the August 26 issue of the scientific journal Nature describe landmark progress in understanding the structure of the ribosome. The ribosome is a complex particle that makes the thousands of proteins that are required for the structure and function of each living cell. Both Nature reports are based on data generated by a scientific technique called x-ray crystallography, performed at the National Synchrotron Light Source, operated by the U.S. Department of Energy's Brookhaven National Laboratory.
The ribosome is the largest and most complex component of a cell to be successfully studied via x-ray crystallography. Researchers from the University of Utah; the Medical Research Council Laboratory of Molecular Biology, Cambridge, England; and Brookhaven Lab presented a model of the small ribosomal subunit known as 30S, from the bacterium Thermus thermophilus. Yale University and Brookhaven researchers reported on the structure of the large ribosomal subunit known as 50S, from the bacterium Haloarcula marismortui. These two independent research efforts point the way for future study of large ribosome complexes.
Malcolm Capel, a Brookhaven National Laboratory biophysicist who is a co-author on both Nature papers, explained, "This research is a technical and scientific tour de force. On a basic science level, these findings represent a giant step on the road to understanding how living organisms make proteins. On a more practical level, many bacterial infections are stopped by antibiotics, which work by inhibiting the production of ribosomes in bacterial cells. Better structural knowledge of ribosomes may lead to developing more effective antibiotics through computer-modeling. Also, ribosomes are used by industry to make important enzymes, which promote chemical reactions. This new structural information may be helpful for developing further industrial applications."
To gain this new data, the researchers grew crystals
'"/>
Contact: Diane Greenberg
greenb@bnl.gov
516-344-2347
DOE/Brookhaven National Laboratory
25-Aug-1999