Molecular cloning, overexpression, purification, crystallization and preliminary X-ray diffraction studies of histidinol phosphate aminotransferase (HisC2) from Mycobacterium tuberculosis

Nasir, N.; Vyas, R.; Chugh, C.; Ahangar, M.S.; Biswal, B.K.

doi:10.1107/S1744309111045386

Figure 5
Amino-acid sequence alignment of Mtb HisC2 and its counterpart from L. innocua. The secondary-structural elements (helices represented by coils, [beta]

-strands by arrows and turns by letter Ts) corresponding to histidinol phosphate aminotransferase from L. innocua are shown. Conserved residues are highlighted with a red background. The sequence alignment was performed by the program MultAlin (Corpet, 1988

) and the figure was generated using the program ESPript (Gouet et al., 1999