 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](ba5127fig4mag.jpg)
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Figure 4
Structure of the α-amanitin-inhibited Pol II elongation complex. (a) Pre-translocation and post-translocation states of the EC. The nucleic acid scaffold used is depicted schematically with respect to the active-site metal ion A (magenta). The colour key is used throughout. (b) Overview of the α-amanitin-inhibited Pol II EC structure. The view is as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) (a). α-Amanitin (stick model), nucleic acids (base in pre-templating position as a stick model), metal A, the bridge helix and the trigger loop (Leu1081 as a stick model) are highlighted using the colour key in (a). Part of the protein is omitted for clarity. (c, d) Bromine anomalous difference Fourier maps (pink net) of the free EC (c) and the α-amanitin-inhibited EC (d). Br atoms are depicted as yellow spheres and their positions are indicated. The view is rotated by 90° around a vertical axis compared with (b). (e) The +1 DNA-template base adopts a pre-templating position. The initial unbiased Fo − Fc difference map for the nucleic acids is shown around the +1 position and is contoured at 2.5σ. The +1 base in the pre-templating site is highlighted in violet. The view is rotated by 90° around a horizontal axis compared with (b). This figure was adapted from Brueckner & Cramer (2008). |
![[Figure 4]](ba5127fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
