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. 2011 Mar-Apr;2(2):60–65. doi: 10.4161/trns.2.2.14366

Figure 2.

Figure 2

(A) Chemical structures of Myx and Lpm. (B) Overlap of the Lpm and Myx binding sites. Amino acids substitutions conferring resistance to Lpm27 are shown in CPK colored in cyan for β subunit (T. thermophilus Q1018, V1087, N1064) and magenta (R613) or dark blue (R87, P526) for β' subunit, σ3.2HL is shown as green ribbons and Myx is shown in ball-and-stick and orange. R613 is shown in two conformations—as in holoenzyme and as in the RNAP-Myx complex.1 (C) Model of the mechanism of Lpm and Myx action. RNAP core is shown as a gray ellipse. The σ subunit is shown in green, region 3.2 is shown as a green triangle, and the β' switch-2 is shown as a blue rectangle. The +1 base of the promoter is indicated by a red circle.