Progress Toward an Understanding of the Structure and Enzymatic Mechanism of the Large Ribosomal Subunit
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Excerpt
The ribosome was discovered in the 1950s (Tissières1974), and by 1969, the last time it was the subject of aCold Spring Harbor Symposium, its role in messengerRNA-directed protein synthesis was well understood. Itsreturn to the Cold Spring Harbor stage in 2001 was precipitated, in part, by a series of field-transforming publications, the first of which appeared in the summer of2000. In August 2000, an atomic structure of the large ribosomal subunit from Haloarcula marismortui derivedfrom a 2.4 Å resolution electron density map was published (Ban et al. 2000; Nissen et al. 2000). A few weekslater, a partially interpreted 3.3 Å resolution electron density map of the small ribosomal subunit from Thermusthermophilus appeared (Schluenzen et al. 2000), and afew weeks after that, a fully interpreted atomic structurefor the same subunit derived from a 3.05 Å resolutionmap (Carter et al. 2000; Wimberly et al. 2000). Most recently, in April 2001, an atomic model was published forthe 70S ribosome from T. thermophilus that is based on a5.5 Å resolution electron density map interpreted usingthe high-resolution structures of the two subunits(Yusupov et al. 2001). These papers, collectively, converted the ribosome field from one perpetually vexed bythe absence of structural information to one in which thestructural information is more than sufficient to formulatefunctional hypotheses...
