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![[Figure 1]](rr5135fig1mag.jpg)
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Figure 1
Catalysis and conformational changes of hlFBPase. (a) Hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate (F6P) by FBPase. The reverse reaction is catalyzed by phosphofructokinase (PFK) at the expense of ATP. (b) Schematic view of the FBPase tetramer and the conformational switch from the active R state (no AMP bound) to the inactive T state (AMP bound). The protomers are labelled C1–C4, with C1/C2 and C3/C4 constituting the functional units that rotate with respect to each other. The active sites for hydrolysis are close to the minor interfaces of these dimers (labelled F6P with the dynamic loop nearby) and the allosteric AMP-binding sites are close to the major interfaces (labelled AMP in the right-hand panel). |
![[Figure 1]](rr5135fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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