3WFO
tRNA processing enzyme (apo form 1)
Summary for 3WFO
| Entry DOI | 10.2210/pdb3wfo/pdb |
| Related | 3WFP 3WFQ 3WFR 3WFS |
| Descriptor | Poly A polymerase, SULFATE ION (2 entities in total) |
| Functional Keywords | terminal nucleotide transferase, transferase |
| Biological source | Aquifex aeolicus |
| Total number of polymer chains | 3 |
| Total formula weight | 182654.84 |
| Authors | Yamashita, S.,Takeshita, D.,Tomita, K. (deposition date: 2013-07-23, release date: 2014-01-01, Last modification date: 2024-03-20) |
| Primary citation | Yamashita, S.,Takeshita, D.,Tomita, K. Translocation and rotation of tRNA during template-independent RNA polymerization by tRNA nucleotidyltransferase Structure, 22:315-325, 2014 Cited by PubMed Abstract: The 3'-terminal CCA (CCA-3' at positions 74-76) of tRNA is synthesized by CCA-adding enzyme using CTP and ATP as substrates, without a nucleic acid template. In Aquifex aeolicus, CC-adding and A-adding enzymes collaboratively synthesize the CCA-3'. The mechanism of CCA-3' synthesis by these two enzymes remained obscure. We now present crystal structures representing CC addition onto tRNA by A. aeolicus CC-adding enzyme. After C₇₄ addition in an enclosed active pocket and pyrophosphate release, the tRNA translocates and rotates relative to the enzyme, and C₇₅ addition occurs in the same active pocket as C₇₄ addition. At both the C₇₄-adding and C₇₅-adding stages, CTP is selected by Watson-Crick-like hydrogen bonds between the cytosine of CTP and conserved Asp and Arg residues in the pocket. After C₇₄C₇₅ addition and pyrophosphate release, the tRNA translocates further and drops off the enzyme, and the CC-adding enzyme terminates RNA polymerization. PubMed: 24389024DOI: 10.1016/j.str.2013.12.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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