A conformation-based intra-molecular initiation factor identified in the flavivirus RNA-dependent RNA polymerase
Fig 2
A comprehensive comparison of the intra-molecular MTase-RdRP interface shown as stereo-pair images.
A) A comparison between the JEV (top) and the first form of DENV2 (bottom) structures. B) A comparison between the DENV3 (top, two models) and the second form of DENV2 (bottom) structures. C) The binding of the second SAH molecule observed in the form 2 of DENV2 structure. The binding pocket is shown as surface representations with conservation scores projected. Thinner sticks show the moderately different SAH binding mode observed in the other NS5 molecule in the crystallographic asymmetric unit. Composite simulated-annealing (SA) omit electron density maps contoured at 1.2 σ are overlaid with the DENV2 models in panels A and B and the SAH molecule in panel C. For the DENV2 structures in panels A and B, the two NS5 molecules in the crystallographic asymmetric unit were superposed and shown as thick and thin representations with the density maps of the thick model overlaid. All structures in panels A and B were superposed but may be presented separately. The coloring scheme is the same as in Fig 1. For panels A and B, the rotational movements correlate the both structure pairs are indicated.