Structural highlights
3avx is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 3avt, 3avu, 3avv, 3avw, 3avy |
| 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
Core Qbeta replicase comprises the Qbeta virus-encoded RNA-dependent RNA polymerase (beta-subunit) and the host Escherichia coli translational elongation factors EF-Tu and EF-Ts. The functions of the host proteins in the viral replicase are not clear. Structural analyses of RNA polymerization by core Qbeta replicase reveal that at the initiation stage, the 3'-adenine of the template RNA provides a stable platform for de novo initiation. EF-Tu in Qbeta replicase forms a template exit channel with the beta-subunit. At the elongation stages, the C-terminal region of the beta-subunit, assisted by EF-Tu, splits the temporarily double-stranded RNA between the template and nascent RNAs before translocation of the single-stranded template RNA into the exit channel. Therefore, EF-Tu in Qbeta replicase modulates RNA elongation processes in a distinct manner from its established function in protein synthesis.
Molecular basis for RNA polymerization by Qbeta replicase.,Takeshita D, Tomita K Nat Struct Mol Biol. 2012 Jan 15;19(2):229-37. doi: 10.1038/nsmb.2204. PMID:22245970[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Takeshita D, Tomita K. Molecular basis for RNA polymerization by Qbeta replicase. Nat Struct Mol Biol. 2012 Jan 15;19(2):229-37. doi: 10.1038/nsmb.2204. PMID:22245970 doi:10.1038/nsmb.2204
