Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10799295 | Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms | 2008 | 11 Pages |
Abstract
The recently reported structures of several nucleotidyl transferases facilitate the study of the catalytic mechanisms of these very diverse enzymes. Numerous structures of CCA-adding enzymes have now revealed all steps in the formation of a CCA tail at the 3â² end of tRNAs. In addition, structures of poly(A) polymerases and uridylyl transferases are now available as binary and ternary complexes with incoming nucleotide and RNA primer. Some of these proteins undergo significant conformational changes after substrate binding. This is proposed to be an indication for an induced fit mechanism that drives substrate selection and leads to catalysis. Insights from recent structures of ternary complexes indicate an important role for the primer molecule in selecting the incoming nucleotide.
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Authors
Georges Martin, Sylvie Doublié, Walter Keller,