 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](mn5082fig1mag.jpg)
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Figure 1
Secondary-structural alignment of enolases. Bacterial (Streptococcus suis), protozoan parasite (Toxoplasma gondii and Plasmodium falciparum), plant (Arabidopsis thaliana) and human enolases are aligned for comparison. The enolases are all nuclear-localized, with the exceptions of human ENO2 and Streptococcus ENO. Human MPB1 is an alternatively spliced form of ENO1 and is truncated at the N-terminal domain. The five conserved active-site residues (His165, Glu174, Glu217, Lys355 and Lys406) are marked by blue arrowheads. The atypical TgENO1 residue replacement E164S at the N-terminus of loop 2 and the interacting residue Tyr270 in loop 3 are indicated by red dots. Conserved positively charged residues on the surface of transcription regulatory enolases are labelled with plus signs (+). Boxed regions are plant-like insertions (red dashes; DI, dipeptide insertion; PI, pentapeptide insertion), catalytic mobile loops (black; L, loop) and plasminogen-binding motifs (blue dashes; PB, plasminogen binding). |
![[Figure 1]](mn5082fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
