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Figure 1 | BMC Structural Biology

Figure 1

From: Dimerization of inositol monophosphatase Mycobacterium tuberculosis SuhB is not constitutive, but induced by binding of the activator Mg2+

Figure 1

Sequence comparison of M. tuberculosis IMPase-like proteins with human IMPase. Sequences were aligned based on the structural superimposition of SuhB and human IMPase using STRAP [53], and formatted using ESPript [54]. Secondary structure elements of SuhB are above the sequence, cylinders representing helices and arrows β-strands, coloured according to Fig. 2A. Full asterisks denote residues coordinating the catalytic Mg2+ sites, triangles indicate residues contacting inositol-1-phosphate in the simulated SuhB-substrate complex. Horizontal boxes indicate disordered parts of the sequence. The grey arrows indicate the positions of strands β1, β2 in the α1-α2 loop ('mobile loop') of human IMPase, with the open asterisk marking the critical lysine residue.

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