 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](hv5185fig1mag.jpg)
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Figure 1
Crystal structure of E. histolytica enolase (EhENO). (a) EhENO is a highly conserved homodimeric enzyme. Secondary-structure elements and a semi-transparent surface are shown in green for subunit A and in orange for subunit B; the N-terminus of molecule B and the C-terminus of molecule A are indicated. (b) A superposition shows the high degree of similarity between the two subunits. However, within the catalytically important loop L1 the subunits differ by up to 10 Å. Virtually no difference can be observed in L2. (c) The figure is coloured according to B factor, where blue denotes a low B factor and red a high B factor. The tube thickness is also related to B factor: a thin tube indicates a low B factor and a thick tube indicates a high B factor. EhENO is a generally rigid molecule as indicated by the relatively low temperature factors. However, higher disorder can be observed within surface-exposed loop structures, presumably owing to increased flexibility in these areas. (d) A superposition of both subunits with tube thickness corresponding to B factor; a thicker tube indicates an increased B factor. Particular flexibility can be observed for L1 of subunit B (L1-B) that shields the active side. |
![[Figure 1]](hv5185fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
