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Thermus thermophilus 70S ribosome (Entries 2wdi & 2wdg)
23S rRNA from Deinococcus radiodurans (Entry 2o43)
Large ribosomal subunit from Haloarcula marismortui (Entry 1ffk)

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Nobel Prize for Chemistry 2009

This year's Nobel Prize for Chemistry has been awarded to Venki Ramakrishnan (UK), Tom Steitz (USA) and Ada Yonath (Israel). These three crystallographers have contributed enormously to our understanding of how the protein production machinery works at the atomic level by determining the detailed three-dimensional structure of so-called ribosomes.

Protein production is one of the major tasks performed by living cells without which there would be no life. Although the information about life is stored in the DNA, it is ribosomes that produce the proteins that are essential for all processes and that control life at the atomic level.

In the recent times, ribosomes have been a major target in the fight against emerging bacterial infections. By designing new antibiotics against bacterial ribosomes we can put a stop to the production of proteins in those organisms and thereby control and eliminate multiresistant bacteria such as MRSA.

Structural biologists around the world have studied the ribosome using various techniques such as Electron Microscopy (EM), and X-ray crystallography. Ribosomes were discovered using early cellular electron microscopy in the 1940s. This important contribution by Albert Claude, Christian de Duve and George E. Palade was recognised by the Nobel Foundation and it awarded them the Nobel Prize in Physiology or Medicine in 1974. The breakthrough in understanding the molecular mechanism came when the atomic structure of the ribosome was determined using the X-ray crystallographic technique by this year's Nobel prize winners Venki Ramakrishnan (UK), Tom Steitz (USA) and Ada Yonath (Israel).

X-ray crystallography is a method for determining the three-dimensional structure of molecules organised within a crystal. The crystal is exposed to a beam of X-rays and the molecules within the crystal diffract the X-rays in specific directions. By studying the diffraction pattern and the intensities and position of the diffracted beam, crystallographers can identify the position and atomic details of the molecules.

The contribution made by crystallographers in particular and structural biologists in general to the field of biology and medicine has been recognised by the scientific community and the Nobel Foundation. The Foundation has awarded more than a dozen Nobel Prizes to this field in the past 50 years. These include the Nobel Prize for Chemistry in 1962 (for studies of the structures of globular proteins) to John Kendrew and Max Perutz and the Nobel Prize in Physiology or Medicine in the same year to Francis Crick, James Watson and Maurice Wilkins (for their studies of "The helical structure of DNA").

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The complete list of all Nobel Prizes awarded to structural biologists is available here.

The wealth of information generated by the structural biology community, be it the atomic details of ribosome, haemoglobin or any other protein or nucleic-acid molecules, is archived in the Protein Data Bank (PDB). This archive was established in 1972 and is now managed by the four Worldwide Protein Data Bank (wwPDB) partners - RCSB and BMRB in the USA, PDBj in Japan and the Protein Data Bank in Europe (PDBe) that was established in 1996 at the European Bioinformatic Institute (EBI) in Cambridge, UK. The four partners ensure that the data is available to the wider scientific community for research and development in the field of biology and medicine. The ribosome structures of one of this year's Nobel Laureates, Dr. Ramakrishnan, were all deposited at the PDBe in Cambridge. More information on the structural studies of ribosome by the three Nobel laureates is available here.

After its discovery in the 1940s, the ribosome remains one of the most frequently studied objects using EM. Ribosomes are one of the largest protein complexes in the living cell and are found in all organisms. Ribosomes are composed of about 65% ribosomal RNA and 35% ribosomal proteins and are about 20nm in size. Similar to the PDB, the data and results generated using EM are archived in the Electron Microscopy Data Bank (EMDB). Established in 2002 at the PDBe, EMDB is nowadays run by a consortium of three institutes, PDBe, RCSB and National Center for Macromolecular Imaging at Baylor College of Medicine. EMDB contains more than 50 data sets on ribosomes, which are available here.

Prof. Ada Yonath started her scientific career 50 years ago as an undergraduate at the Hebrew University in Jerusalem, Israel. She is the recipient of numerous awards and is a member of many national and international scientific organisations, including the European Molecular Biology Organisation (EMBO). After a career that has spanned the globe, she is presently the director of the Kimmelman Center for Biomolecular Assemblies at the Weizmann Institute of Science in Rehovot, Israel. The ribosome was central to her research from the initial crystallisation studies in the late 1970s to her first electron density map of the small ribosomal subunit from Thermus thermophilus, constructed at 4.5 Å (PDB entry 1dv4) and continuing in recent studies of the interaction of antibiotics with the large ribosomal subunit (PDB entries 2o43, 2o44 and 2o45).

Prof. Tom Steitz is one of the most outstanding structural biologists today, with close to 200 structures in the PDB. He got his PhD from Harvard University. He spent three post-doctoral years working at the MRC Laboratory of Molecular Biology in Cambridge (UK), where the third recipient of this Nobel prize, Dr. Ramakrishnan works at present. He joined Yale University in 1970 and is now Sterling Professor of Molecular Biophysics and Biochemistry, Professor of Chemistry, an investigator of the Howard Hughes Medical Institute, and a recipient of numerous prestigious scientific awards. His long scientific career has been focused on studying the structural basis of the molecular and chemical mechanisms by which proteins and nucleic acids exert their biological functions. His research led to the first high-resolution crystal structure of the large ribosomal subunit from Haloarcula marismortui (PDB entry 1ffk) and was published in the year 2000.

Dr. Venki Ramakrishnan was born in India where he started his physics studies at the Maharaja Sayajirao University of Baroda. After receiving his PhD from the University of Ohio in 1976, he spent a transition year shifting his research interest from theoretical physics to biology. He now leads a strong research group at the MRC Laboratory of Molecular Biology in Cambridge (UK), that is studying the structure and function of the ribosome. He has determined the structure of the Thermus thermophilus 30S ribosomal subunit in complex with several antibiotics (PDB entry 1fjg). Dr. Ramakrishnan's research into the ribosome and its complexes with antibiotics, initiation factor IF1, as well as cognate and near-cognate tRNA has resulted in an extensive body of publications, almost 70 entries in the PDB and has contributed significantly to our understanding of this vital organelle. Dr. Ramakrishnan is a Fellow of the British Royal Society and a member of EMBO.

Timeline of ribosome related structure releases (Drag or double-click timeline to navigate.)

This page was created by the following members of the PDBe team: Miri Hirshberg, Sameer Velankar, Jawahar Swaminathan, Glen van Ginkel, Gaurav Sahni, Harry Boutselakis, Christoph Best, Gerard Kleywegt. For more information about PDBe or the ribosome structures deposited in the PDB, please contact Sameer or Jawahar.