 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 4]](gx5109fig4mag.jpg)
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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 Cα 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. |
![[Figure 4]](gx5109fig4.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
