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![[Figure 6]](rr5135fig6mag.jpg)
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Figure 6
Structural variation of hlFBPase protomers as the origin of pseudo-symmetry. (a) Side-on view of the FBPase dimers shifted along the rNCS axis shown in Fig. 3 ![[link]](../../../../../../logos/arrows/d_arr.gif) (b). The colour code also follows that in Fig. 3(b). The diameter of the backbone trace corresponds to the mean B value of this region, indicating possible flexibility at the N-terminus (labelled) and surface-loop regions. The asterisk denotes a missing loop region (residues 22–26). (b) View rotated 90° compared with that in (a), showing the lateral displacements of the dimers perpendicular to the rNCS axis in the ab plane. (c) Superposition of the two hlFBPase tetramers onto one protomer (blue and orange) shows little differences in this orientation. The twofold axes of the almost D2-symmetric tetramers are marked in black. Important sites are shown as transparent spheres. Small spheres, allosteric AMP-binding sites; grey central sphere, second allosteric site; other large spheres, active and fructose 2,6-bisphosphate-binding sites. (d) A rotation by 90° compared with (c) reveals a tilted arrangement of dimers. The rotation axes for the upper dimers are drawn as rods, coloured according to one of the protomers, and differ in direction by 2.2°. (e) Top view along the rNCS axes shows displacements of the protomers in excess of 2 Å. |
![[Figure 6]](rr5135fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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