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

Table 3 Description of the interface signature motifs.

CLASS*	FRACTION OF CONSERVED/PARTIALLY/NON CONSERVED RESIDUES AT THE INTERFACE FORMING THE MOTIF**	^#SEQUENCE NUMBER AND RESIDUE NAMES OF THE SIGNATURE MOTIF
II	27/242 (11.16%)	5 *V/L(A/B)* 8F(A/B) 28G/T(A/B)30 *N/H/K(A/B)* 32D(A/B) 116A/E(A/B)55H(A/B) 59H(A/B) 128H(A/B)
III	24/206 (11.65%)	4V(A/B) 7F(A/B) 57E(A) 83G(A) 120A(A/B) 54H(A/B) 58(A/B) 132H(A/B)
IV	30/183 (16.39%)	10F(A) 30T(A/B) 32K/R/S(A) 34D(A/B)76D(A/B) 87Y(A/B) *117I(B)* 57H(B) 61H(B) 131H(B)
V	33/218 (15.14%)	7F(A) 10 D(B) 27 T/G(A/B)29 *K/H(A/B)* 31D(A/B) 55T(B) 57E(B) 84 *R/K(A/B)* 54H(A/B) 58H(A/B) 134H(A/B)
VI	45/214 (21.02%)	28Q/P(A)29 *K/H(A/B)* 31D(A/B) 33I(A) 57E(B) 72I(B) 77F(A) 80R(B) 84H(A) 88W(A/B) 126N(A) 129D(A) 54H(B) 58H(B) 130H(B)

The numbering of residues is done for one representative member of each class (1j6x-class II, 1j98-class III, 1inn-class IV, m1vib-class V, and m1lac-class VI). Complete conservation of the residues is indicated in bold and the bold italics indicate semi-conservative mutation within the class; the normal font indicates no conservation within the class. Fraction of conserved/partially/non conserved residues at the interface that forms the interface signature motif is also given. The conservation information is based on the proteins taken in this study and within a class (approximately the residue conservation was verified to be similar in a larger dataset of available sequences in classes such as III and VI).
* Any definite motif was absent in class I
# (A/B) refers to the residues from both the chains. (A) or (B) refers to the residues from a single chain.** (Number of conserved/partially/non conserved residues forming the motif)/(total number of interface residues).

ISSN: 1472-6807