Characterization of M. tuberculosis SerB2, an Essential HAD-Family Phosphatase, Reveals Novel Properties
Figure 1
Sequence alignment and modeling.
(A) Sequence alignment of MtSerB2 with sequences of Phosphoserine phosphatases from M. avium (MavSerB), P. gingivalis (PgSerB653), P. gingivalis (PgSerB1170), M. tuberculosis (MtSerB1), MjPSPase (M. janaschii) and HsPSPase (Homo sapiens). Three conserved motifs of the PSP domain are shown in red. The ACT1 and ACT2 domains are colored blue and green respectively Secondary structural elements are also indicated. The sequences highlighted in red represents high consensus whereas those in blue represents low consensus (B) Modeled structure of MtSerB2. MtSerB2 structure was modeled using M. avium SerB structure (PDB: 3P96) and Modeler 9.10. The monomeric and dimeric associations are depicted and the individual domains are labelled. Gly residues important for binding ligands in ACT domains are shown in ‘stick’ representation and labeled for clarity. Selected catalytic residues on the PSP domain are also labeled and depicted.