Figure 1

Schematic representation of the proposed pathway for MPT formation from cPMP and sequence analysis of MoaX. (A) MPT synthesis is catalyzed by the heterotetrameric MPT synthase, which is made up of two MoaD (Green-Active, Yellow-Inactive) and two MoaE (Red) subunits. S – Sulphur. The MPT synthase encoding genes in M. smegmatis and M. tuberculosis are shown to highlight the multiplicity of homologues in M. tuberculosis. Adapted from [14,17,22]. (B) Sequence alignment of E. coli MoaD (ECDH10B_0852) and MoaE (ECDH10B_0853), Mtb MoaD1 (Rv3112), Mtb MoaD2 (Rv0868c), Mtb MoaE1 (Rv3119), Mtb MoaE2 (Rv0866) and MoaX (Rv3323c) proteins. Conserved Gly residues are shown in red, these correspond to positions 81 and 82 in MoaX. The M. tuberculosis MoaX sequence is highlighted in bold; the MoaD component is shown in the green box and the MoaE component in the red box. The Alignment was generated using sequences obtained from Tuberculist (http://genolist.pasteur.fr/TubercuList/) and the Clustal Omega (http://www.ebi.ac.uk/Tools/msa/clustalo/) online alignment tool.