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Figure 4 | BMC Structural Biology

Figure 4

From: Functional correlation of bacterial LuxS with their quaternary associations: interface analysis of the structure networks

Figure 4

Triangular pattern at the dimer interface. The pattern comprises of the two active sites clusters I and II and the apex cluster at the top vertex of LuxS. (a) Isosceles triangular pattern of the amino acid residues in the interface clusters (cluster I, II and apex cluster) well-organized at the dimer interface for m1eco. The edges of the triangle are calculated to be 31.66, 31.42 and 13.09 Ã… for active-site cluster I, apex cluster, and active site cluster II moving clockwise, (b) Isosceles triangular pattern of the amino acid residues in the interface cluster is distorted at the dimer interface for the probiotics and some extremophiles, as shown here for the probiotic m1lac. The edge between apex cluster and active site cluster II is 31.33 Ã… but active-site cluster I is missing from the interface cluster as the three His (chain A) have moved away from Phe (chain B) by 15 Ã… as compared to 8 Ã… distance between Phe (chain B) and the three His (chain A). The backbone is represented by transparent new cartoon and the amino acid residues at the vertices of the triangle as van der Waal's spheres; each monomer and its amino acid residues coloured differently. Residues from chain A are coloured Blue and those from B are coloured Red. An imaginary line is drawn across the interface in yellow and the distances between His 58 (CB) and Phe 7 (CB) are approximately given for m1lac.

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