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![[Figure 1]](dw5156fig1mag.jpg)
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Figure 1
Overall fold of the muscle FBPase tetramer in the T (a) and R (b) states shown in cartoon representation with subunits, labelled C1–C4, in different colours. The secondary-structure elements are assigned according to DSSP (Kabsch & Sander, 1983  ). Four AMP molecules, shown as space-filling models, are present, one in each nucleotide-binding site of the T form. (c) and (d) show a top view of the structures in (a) and (b), respectively, with the definition of the κ angle (see text) between the vectors joining the Cα atoms of Leu30 (black or grey dots) in subunits C2→C1 (black arrow) and C3→C4 (grey arrow). (e, f) Overall architecture of the muscle FBPase tetramer in the T (e) and R (f) states, shown in surface representation. Each subunit is divided into two domains: the allosteric domain (grey) and the catalytic domain (orange). Hydrophobic residues forming the central cavity in the middle of the tetramer are marked in green. To show the details of the central hydrophobic cavity, the catalytic loop L2 has been omitted in the T state (c), while in the R state (d) the forefront subunit C1 is not shown. |
![[Figure 1]](dw5156fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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