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. 2010 Jun 18;29(15):2527–2537. doi: 10.1038/emboj.2010.135

Figure 1.

Figure 1

Modelling of the mutations conferring resistance to Lpm in the structure of the T. thermophilus RNAP. (A) Chemical structure of Lpm. (B) Structure of the core RNAP in complex with scaffold DNA (Vassylyev et al, 2007) with the amino acids substitutions conferring resistance to Lpm shown as CPK. Numbering corresponds to T. thermophilus and E. coli (in brackets) enzymes. The β′ switch-2 (magenta), β switch-3 (cyan), β′ Lid (orange), β′ Zn-finger (brown) and β clamp (purple) elements of the clamp are shown as ribbons. DNA is shown in red (template strand) and dark blue (non-template strand), and RNA is indicated in yellow. Position of the active site is marked by magnesium ion (red sphere). RNAP subunits: β′—khaki, β—blue, α—gold, ω—grey. Molecular graphics images were produced using the UCSF Chimera package (Pettersen et al, 2004).