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Mechanism of Poly(A) Polymerase: Structure of the enzyme-MgATP–RNA ternary complex and kinetic analysis
We report the 1.8 Å structure of yeast poly(A) polymerase (PAP) trapped in complex with ATP and a five residue poly(A) by mutation of the catalytically-required aspartic acid 154 to alanine. The enzyme has undergone significant domain movement and reveals a closed conformation with extensive interac...
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| Main Authors: | , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2007
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2032019/ https://ncbi.nlm.nih.gov/pubmed/17850751 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2007.07.010 |
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