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. 2008 Feb 13;3(2):e1602. doi: 10.1371/journal.pone.0001602

Figure 1. Alignment of OxyR homologs from different organisms.

Figure 1

Using CLUSTAL W software aligned amino acid sequences of the Streptomyces coelicolor A3(2), Neisseria gonorrhoeae, E. coli, and D. radiodurans. Identical amino acids are highlighted in black, and conserved residues are highlighted with grey. The DrOxyR helix-turn-helix region has four conserved residues (R4, L32, S33 and R50) [17]. At its LysR-substrate binding domain, D142 and R273 possibly define an activating region on OxyR (contact with RNA polymerase)[18], A233 residue is involved in tetramerization[17], V110, L124, and A233 form a hydrophobic core[58]. Numbering is based on the E. coli OxyR sequence.