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The structure of a ribozyme catalyzing the Diels-Alder reaction shows how an RNA can form carbon-carbon bonds between two small molecules. The RNA (ribbon diagram) resembles the Greek letter λ, and uses structural principles similar to those found in proteins catalyzing Diels-Alder reactions. pp 218-224; News and Views pp 206-208. Cover design by E. Boyle.
The first structure of a ribozyme that catalyzes the stereospecific carbon-carbon bond formation between two small molecules shows how an RNA active site can perform the synthetically important Diels-Alder reaction. Surprisingly, the ribozyme active site shares structural features with proteins that catalyze the same reaction.
Glutamate receptor ion channels are multidomain membrane proteins that mediate excitatory synaptic responses in the brain and spinal cord. Single-particle electron microscopy reveals their molecular envelope and how this changes during desensitization.
Two recent papers characterize a protein complex that is part of the budding yeast kinetochore, the specialization that links chromosomal DNA with one or more spindle microtubules. Both studies present convincing evidence that this complex can assemble into rings or helices that wrap around microtubules.
The tumor suppressor protein BRCA2 promotes efficient repair of damaged chromosomes by homologous recombination, and it does so by influencing the activity of the Rad51 recombinase. A new biochemical study on the Ustilago maydis BRCA2 ortholog Brh2 sheds light on the molecular function of this tumor suppressor in the Rad51-mediated homologous recombination reaction.
Although RecA filaments are required for genetic recombination, it now seems that they are not required for translesion synthesis and that they actually inhibit this process. This finding along with elegant biochemical studies of mutant proteins moves us closer to discerning the direct role of RecA protein in SOS mutagenesis.