journal menu
![[Figure 3]](jc5034fig3mag.jpg)
|
|
Figure 3
Sequence alignment of MurC proteins. The amino-acid sequences shown are for MurC from M. bovis (MbMurC; gb:54037857), H. influenzae (HiMurC; gb:1171071), T. maritima (TmMurC; gb:6919931), Y. pestis (YpMurC; gb:115346363) and E. coli (EcMurC; gb:127536). The α-helices and β-sheets are indicated in red and blue, respectively, in their order of appearance in the MbMurC structure. The glycine-rich loop (GRL) is indicated by a black dotted box. The UDP-, ATP- and amino-acid-binding domains are presented on orange, blue and green backgrounds. Identical residues are marked by `*'. Strongly conserved (scoring >0.5 in the Gonnet PAM 250 matrix) and weakly conserved (scoring ≤0.5 in the Gonnet PAM 250 matrix) residues are indicated by `:' and `.', respectively. The sequence alignment was prepared using Clustal Omega (Sievers et al., 2011  ). |
![[Figure 3]](jc5034fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
