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Figure 3 | BMC Research Notes

Figure 3

From: Characterisation of a natural variant of the γ-butyrolactone signalling receptor

Figure 3

Amino acid sequence alignment and deduction of functional domains for residues of CprB, ScbR M145 and ScbR M600 . The deduction of functional domains and residues is based on CprB data from [14]. The amino acid sequences represent monomers of each protein. Peptides readily detected by MALDI-TOF analysis in ScbRM145 (spot 1 in Figure 1A) but not in ScbRM600 (spot 2 in Figure 1B) are indicated by black bars (ScbR amino acids 48–58 and 119–126). Residues forming α-helices are boxed and labelled. Boxes are shaded for α-helices 4–8 involved in the formation of the γ-butyrolactone binding pocket. Bold boxes for α-helices 8 and 9 indicate their role in dimerization. Dashed boxes mark the DNA binding domain (α1-3) with α2 and α3 forming a helix-turn-helix motif, and the regulatory domain (α5-10). A highly conserved tryptophan residue directly involved in ligand binding (W127 in CprB; W121 in ScbR) is underlined. The mutated amino acid residue 120 is indicated in bold for ScbRM145 (R120) and for ScbRM600 (S120).

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