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. 2006 Dec 19;35(2):634–647. doi: 10.1093/nar/gkl686

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© 2006 The Author(s).

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Dual binding of Rpb5 to Rpb1 (A) View of the salt bridge system involving R200 and R212 (Rpb5) and six Rpb1 amino acids: E870, D871 (Rpb1-β25), E1342 and R1345 (Rpb1-α46), R1366 and D1373 (Rpb1-α47). Drawing based on the PDB crystallographic coordinates 1I6H (41), with Hydrogen atoms recalculated by the PDB-viewer programme. The Rpb5 domain is in blue, and the two Rpb1 parts in green. (B) Spatial organization of Rpb5, the Rpb1-β24/25-fold and the Bridge helix (Rpb1-α25), using the same orientation as in Figure 1. Rpb5 is shown in blue, with the eukaryotic backbone domain shown as a thin line. R200 and R212 are space-filled. Rpb1-β24/25 and Rpb1-α25 are shown in green and red, respectively. (C) Conservation of the Rpb1-β24/25 sequence. Species symbols as in Figure 4. Conserved amino acids are in red.