3vnv

Complex structure of viral RNA polymerase II

spinqualitylabelsall models 3vnv, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vnv is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CH1 Related: 3agp, 3agq, 3vnu Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [EFTS_ECO57] Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity). Publication Abstract from PubMed The genomic RNA of Qbeta virus is replicated by Qbeta replicase, a template-dependent RNA polymerase complex. Qbeta 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 Qbeta replicase has remained elusive. We determined the structure of a complex that includes Qbeta 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 Qbeta replicase is the RNA and protein ribonucleoprotein complex. Mechanism for template-independent terminal adenylation activity of Qbeta replicase.,Takeshita D, Yamashita S, Tomita K Structure. 2012 Oct 10;20(10):1661-9. doi: 10.1016/j.str.2012.07.004. Epub 2012, Aug 9. PMID:22884418 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor

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