4r71

Structure of the Qbeta holoenzyme complex in the P1211 crystal form

spinqualitylabelsall models 4r71, resolution 3.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4r71 is a 6 chain structure with sequence from Escherichia coli K-12 and Escherichia virus Qbeta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EFTU2_ECOLI This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118]EFTS_ECOLI 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.[HAMAP-Rule:MF_00050] Publication Abstract from PubMed Upon infection of Escherichia coli by bacteriophage Qbeta, the virus-encoded beta-subunit recruits host translation elongation factors EF-Tu and EF-Ts and ribosomal protein S1 to form the Qbeta replicase holoenzyme complex, which is responsible for amplifying the Qbeta (+)-RNA genome. Here, we use X-ray crystallography, NMR spectroscopy, as well as sequence conservation, surface electrostatic potential and mutational analyses to decipher the roles of the beta-subunit and the first two oligonucleotide-oligosaccharide-binding domains of S1 (OB1-2) in the recognition of Qbeta (+)-RNA by the Qbeta replicase complex. We show how three basic residues of the beta subunit form a patch located adjacent to the OB2 domain, and use NMR spectroscopy to demonstrate for the first time that OB2 is able to interact with RNA. Neutralization of the basic residues by mutagenesis results in a loss of both the phage infectivity in vivo and the ability of Qbeta replicase to amplify the genomic RNA in vitro. In contrast, replication of smaller replicable RNAs is not affected. Taken together, our data suggest that the beta-subunit and protein S1 cooperatively bind the (+)-stranded Qbeta genome during replication initiation and provide a foundation for understanding template discrimination during replication initiation. Structural basis for RNA-genome recognition during bacteriophage Qbeta replication.,Gytz H, Mohr D, Seweryn P, Yoshimura Y, Kutlubaeva Z, Dolman F, Chelchessa B, Chetverin AB, Mulder FA, Brodersen DE, Knudsen CR Nucleic Acids Res. 2015 Dec 15;43(22):10893-906. doi: 10.1093/nar/gkv1212. Epub, 2015 Nov 17. PMID:26578560 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures RNA polymerase 3D structures Ribosomal protein S1

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