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. Author manuscript; available in PMC: 2013 May 29.
Published in final edited form as: J Mol Biol. 2006 Apr 6;359(3):624–645. doi: 10.1016/j.jmb.2006.03.050

Figure 7.

Figure 7

Comparison of the CheY backbone conformations in the CheY-CheZ200-214 complexes with those in inactive and active CheY. δ3 plots are shown for main chain atoms of CheY in BeF3-free F432YZ200-214 (cyan), BeF3-bound F432YZ200-214 (deep blue) and BeF3-bound P2(1)2(1)2YZ200-214 (orange) following “sieve-fit” superposition with inactive Mg2+-bound CheY (2CHE)14 (upper panel), resulting in overall r.m.s.d. values of 0.50 Å, 0.48 Å and 0.98 Å, respectively and with BeF3-activated CheY (1FQW)15 (lower panel), resulting in overall r.m.s.d. values of 0.80 Å, 0.77 Å and 0.35 Å, respectively. The BeF3-free F432YZ200-214 and the “meta-active” conformer of the BeF3-bound F432YZ200-214 structures solved from crystals grown in Tris (pH 8.4) were used for δ3 and r.m.s.d. calculations, shown here. Key active-site and switch residues are highlighted on the plots by square symbols. The secondary structure of CheY is plotted for reference.