Structural studies of a bacterial tRNA(HIS) guanylyltransferase (Thg1)-like protein, with nucleotide in the activation and nucleotidyl transfer sites.
All nucleotide polymerases and transferases catalyze nucleotide addition in a 5' to 3' direction. In contrast, tRNA(His) guanylyltransferase (Thg1) enzymes catalyze the unusual reverse addition (3' to 5') of nucleotides to polynucleotide substrates. In eukaryotes, Thg1 enzymes use the 3'-5' addition...
محفوظ في:
| المؤلفون الرئيسيون: | , , , , |
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| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
Public Library of Science (PLoS)
2013-01-01
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| سلاسل: | PLoS ONE |
| الوصول للمادة أونلاين: | http://europepmc.org/articles/PMC3701042?pdf=render |
| الوسوم: |
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