Structure of 5-formyltetrahydrofolate cyclo-ligase from Bacillus anthracis (BA4489)

Meier, C.; Carter, L.G.; Winter, G.; Owens, R.J.; Stuart, D.I.; Esnouf, R.M.

doi:10.1107/S1744309107007221

Figure 4
Sequence and structural alignments of prokaryotic 5-formyl-THF cyclo-ligase enzymes. (a) Annotated sequence alignment of the B. anthracis, B. subtilis and M. pneumoniae 5-formyl-THF cyclo-ligases. The residue numbering refers to the B. anthracis sequence, with secondary-structural assignments shown above the alignment. (b) Orthogonal views of the superposition of the corresponding crystal structures (calculated using the program SHP; Stuart et al., 1979

). The B. anthracis structure is shown in a red semitransparent cartoon representation; the crystal structures for the B. subtilis (PDB code 1ydm ) and M. pneumoniae (PDB code 1u3g ) enzymes are shown as coloured C [alpha]

traces in blue and green, respectively. The overall fold of the protein is tightly conserved, except for the 20 amino-acid insertion at the bottom right of the right-hand figure.