Figure 5
(a) Superposition of the A domain (red) and B domain (blue) of LdtMt2. The major differences in the core fold (indicated by >) are the [alpha]-helix (residues 180-187) inserted between [beta]-strands [beta]2 and [beta]3, which is not present in the A domain, and the longer loop connecting [beta]6 and [beta]7 in the B domain. (b) Superposition of domain A (red) from LdtMt2 with the homologous domain of the endo-[beta]-1,4-mannanase from C. fimi (light blue; PDB entry 2x2y ). Conserved residues of LdtMt2 are shown as yellow stick models. Five threonine side chains on the surface of the three-stranded [beta]-sheet show a similar pattern in the mannanase and the A domain of LtdMt2 and are shown as blue sticks.  [article HTML]