Structure of LdtMt2, an l,d-transpeptidase from Mycobacterium tuberculosis

Böth, D.; Steiner, E.M.; Stadler, D.; Lindqvist, Y.; Schnell, R.; Schneider, G.

doi:10.1107/S0907444912049268

Figure 5
(a) Superposition of the A domain (red) and B domain (blue) of Ldt_Mt2. The major differences in the core fold (indicated by >) are the [alpha]

-helix (residues 180-187) inserted between [beta]

-strands

2 and

3, which is not present in the A domain, and the longer loop connecting [beta]

6 and

7 in the B domain. (b) Superposition of domain A (red) from Ldt_Mt2 with the homologous domain of the endo- [beta]

-1,4-mannanase from C. fimi (light blue; PDB entry 2x2y ). Conserved residues of Ldt_Mt2 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 Ltd_Mt2 and are shown as blue sticks.