Fig. 4: Cryo-EM structure and analysis of Augmin antiparallel dimer assembly. | Nature Communications

Fig. 4: Cryo-EM structure and analysis of Augmin antiparallel dimer assembly.

From: Cryo-EM structures of plant Augmin reveal coiled-coil assembly, antiparallel dimerization, and NEDD1 binding

Fig. 4: Cryo-EM structure and analysis of Augmin antiparallel dimer assembly.

A Top: 2D class averages showing ~65 nm antiparallel organization of extended domains extracted in 450 pixels box at 1.76 Å/pixel. Bottom: Low-resolution reconstruction with focused refinement of dimerization interface. B Detailed structural analysis of extended region dimer. Left: Side view of segmented reconstruction with colored subunit organization. Middle: 90° rotated view showing subunit arrangement. Right: Isolated model highlighting subunit organization at dimer interface. C Dimer interface analysis showing protomer organization. Red/blue: individual protomers. Yellow: Interface region between protomers. D Conformational changes in dimer formation. Splayed view of protomers showing AUG1,3,4,5 organization. Interface zones highlighted in red at foot and belly regions. Arrows indicate domain movements during dimerization. E Monomer-to-dimer transition analysis. Left: Single protomer structure. Middle: Overlay of monomeric and dimeric states. Right: Vector representation of conformational changes in tripod, belly, and leg regions.

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