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(A ) The phosphate-binding loop and interface loop frame opposite sides of the FAD-binding pocket.
The largest conformational differences are limited to two local structural elements, namely the phosphate-binding loop and the interface loop.
(B and C ) The interface loop and phosphate-binding loop are also sites of high structural plasticity.
The largest structural variations take place in two local regions, the interface loop next to the FAD-binding pocket and a serine-rich loop neighboring a secondary pocket (see below).
Minor comments to address: 1) Figure 4 figure supplement 2 can be cited when the authors refer to the structural variations of the interface loop and a serine-rich loop.
The FAD-binding pocket is framed by the phosphate-binding loop and the interface loop on opposite edges, whereas the secondary pocket is guarded by the serine loop on one side.
Similar(52)
Overall, the results suggest that the β-interface loop in CE7 enzymes is dispensable for the oligomeric assembly.
This element called the β-interface loop contributes 20 30% of the total buried surface area at intersubunit interfaces of the functional hexameric state.
All structures display a structurally well-conserved homodimeric flavodoxin-like fold where the principal differences are noted for the precise length and conformation of mainly the dimer-interface loops delineating the flavin-binding pocket.
Overall, the structure is very similar to caspase 3 (V266H), with movements along the protein surface between the interface and loop 1 (Supplementary Figure S6 at http://www.bioscirep.org/bsr/032/bsr0320401add.htm).htm
Together with the kinetics results, these structural and dynamics data suggest an inhibitory mechanism in which binding at the dimer interface impacts loop movements that are required for product release.
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