Structure of the Qbeta replicase holo complex

Structure of the Qbeta holo complex

Crystal structure of the Qbeta holo complex bound to ribosomal protein S1

Today, our lab in collaboration with the labs of Charlotte Knudsen and Frans Mulder, published a paper describing crystal and NMR structural studies of the Qbeta replicase holo complex bound to ribosomal protein S1. In the paper, we show how S1 interacts with the viral replicase along with the two other host proteins, elongation factors EF-Tu and EF-Ts, to generate the fully functional, viral replicase enzyme. Using NMR, we further show how  two of the OB domains of S1 are involved in binding viral RNA during replication.

For more information, have a look at the paper in Nucleic Acids Research.

Gytz, H., Mohr, D., Seweryn, P., Yoshimura, Y., Kutlubaeva, Z., Dolman, F., Chelchessa, B., Chetverin, A. B., Mulder, F. A. A., Brodersen, D. E. and Knudsen, C. R. (2015) ” Structural basis for RNA-genome recognition during bacteriophage Qβ replication”, Nucleic Acids Res, 43(22):10893-906.