 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](nj5313fig2mag.jpg)
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Figure 2
Structural and primary-sequence alignment of FolM alternative dihydrofolate reductase 1 from B. suis (PDB entry 5tgd) and B. canis (PDB entry 5bt9) with the molecular-replacement search model 3-oxoacyl-(acyl carrier protein) reductase from Bacillus anthracis (PDB entry 2uvd) and protozoan structures (Trypanosoma brucei pteridine reductase with cyromazine, PDB entry 2x9n; T. brucei pteridine reductase ternary complex with cofactor and inhibitor, PDB entry 4cm8; T. cruzi pteridine reductase, PDB entry 1mxf). The secondary-structure elements are shown as follows: α-helices are shown as large coils, 310-helices are shown as small coils labeled η, β-strands are shown as arrows labeled β and β-turns are labeled TT. Identical residues are shown on a red background, with conserved residues in red and conserved regions in blue boxes. Regions of greatest variability within the core of the protein are identified with brown lines and labeled SBC due to their proximity to the substrate-binding cavity. |
![[Figure 2]](nj5313fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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