Figure 1.

Alignment of IMPases. The M. tuberculosis H37RvIMPases were aligned using ClustalW. (A) Complete sequences. Motifs shown in bold; (B) Prosite motifs: '*' identical residues in all sequences; ':' conserved substitutions; '.' semi-conserved substitutions. Sequences were obtained from webcite. Reported Prosite motifs are 1 (N-terminal; PS00629): [FWV]-x(0,1)- [LIVM]-D-P- [LIVM]-D- [SG]- [ST]-x(2)- [FY]-x- [HKRNSTY]; and 2 (C-terminal; PS00630): [WYV]-D-x- [AC]- [GSA]- [GSAPV]-x- [LIVFACP]- [LIVM]- [LIVAC]-x(3)- [GH]- [GA]. Residues that are not encompassed by these motifs are in bold italics. Arrows indicate putative metal binding aspartate and isoleucine residues reported for human IMPase [55]. The underlined residue shows the aspartate mutated in this study, which is equivalent to mutations introduced into the E. coli and human proteins (see main text).

Movahedzadeh et al. BMC Microbiology 2010 10:50   doi:10.1186/1471-2180-10-50
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