4FWT
Complex structure of viral RNA polymerase form III
Summary for 4FWT
Entry DOI | 10.2210/pdb4fwt/pdb |
Related | 3AGP 3AGQ 3VNU 3VNV |
Descriptor | Elongation factor Ts, Elongation factor Tu, LINKER, Q beta replicase, RNA (5'-R(*C*CP*CP*UP*AP*CP*CP*C)-3'), RNA (5'-R(*GP*GP*GP*UP*AP*GP*GP*G)-3'), ... (6 entities in total) |
Functional Keywords | rna polymerase, translation, transferase-rna complex, transferase/rna |
Biological source | Escherichia coli O157:H7 More |
Total number of polymer chains | 3 |
Total formula weight | 147104.18 |
Authors | Takeshita, D.,Tomita, K. (deposition date: 2012-07-02, release date: 2012-08-08, Last modification date: 2023-11-08) |
Primary citation | Takeshita, D.,Yamashita, S.,Tomita, K. Mechanism for template-independent terminal adenylation activity of Q beta replicase Structure, 20:1661-1669, 2012 Cited by PubMed Abstract: The genomic RNA of Qβ virus is replicated by Qβ replicase, a template-dependent RNA polymerase complex. Qβ replicase has an intrinsic template-independent RNA 3'-adenylation activity, which is required for efficient viral RNA amplification in the host cells. However, the mechanism of the template-independent 3'-adenylation of RNAs by Qβ replicase has remained elusive. We determined the structure of a complex that includes Qβ replicase, a template RNA, a growing RNA complementary to the template RNA, and ATP. The structure represents the terminal stage of RNA polymerization and reveals that the shape and size of the nucleotide-binding pocket becomes available for ATP accommodation after the 3'-penultimate template-dependent C-addition. The stacking interaction between the ATP and the neighboring Watson-Crick base pair, between the 5'-G in the template and the 3'-C in the growing RNA, contributes to the nucleotide specificity. Thus, the template for the template-independent 3'-adenylation by Qβ replicase is the RNA and protein ribonucleoprotein complex. PubMed: 22884418DOI: 10.1016/j.str.2012.07.004 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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