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Figure 3
Chain-wise structural superposition reveals discrete conformational states and coordinated motion in the MATα24βV12 complex. Structural superposition of the three cryoEM classes of MATα24βV12, wobbly, syn and anti, was performed using MATα2 Chain B as a reference (red star) to assess relative conformational changes across the complex. The three pairwise comparisons are shown: wobbly versus syn (left), anti versus syn (middle) and wobbly versus anti (right). MATα2 protomers (Chains A–D) and MATβV1 subunits (Chains E and F) are labelled. In all comparisons, the MATβV1 subunit at the northern end (Chain E) and the adjacent MATα2 protomers (Chains A and B) superimpose closely, indicating a rigid, well anchored interface. In contrast, the MATβV1 subunit at the southern end (Chain F) exhibits pronounced positional variability, accompanied by subtle but consistent shifts in the neighbouring MATα2 protomers (Chains C and D), highlighting propagation of motion into the catalytic core. |
ISSN: 2052-2525
CRYO | EM
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