Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP.

@article{Bard2000StructureOY,
  title={Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP.},
  author={J. D. Bard and Alexander M. Zhelkovsky and Steffen Helmling and Thomas N Earnest and Claire L. Moore and Andrew Bohm},
  journal={Science},
  year={2000},
  volume={289 5483},
  pages={1346-9}
}
Polyadenylate [poly(A)] polymerase (PAP) catalyzes the addition of a polyadenosine tail to almost all eukaryotic messenger RNAs (mRNAs). The crystal structure of the PAP from Saccharomyces cerevisiae (Pap1) has been solved to 2.6 angstroms, both alone and in complex with 3'-deoxyadenosine triphosphate (3'-dATP). Like other nucleic acid polymerases, Pap1 is composed of three domains that encircle the active site. The arrangement of these domains, however, is quite different from that seen in… CONTINUE READING

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