Fig. 5: The cryo-EM structure of the RE-RE Hermes transpososome. | Nature Communications

Fig. 5: The cryo-EM structure of the RE-RE Hermes transpososome.

From: Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding

Fig. 5

a Sequence of the top strand of the 8 + TIR-RE + 30 DNA (RE-DNA). The bases in gray were absent on the top strand, but their complements were present in the bottom strand. The terminal inverted repeat (TIR) is in italic, the subterminal repeats STR0 to STR2 are underlined, and their orientation is indicated by arrows. b Example of selected 2D classes (box size is 250 Å) from the data processing in RELION74,75,76. The transposase dimers (Hd) are marked with white arrowheads and the RE-DNAs are indicated with blue arrowheads. c The best 3D class of the transpososome is composed of four Hermes dimers marked A to D, and two RE-DNAs. d The map of the core of the RE-RE Hermes transpososome (5.1 Å resolution). No clear density for DNA-bound or free BED domains is present. The map was sharpened and denoised with DeepEMhancer85. The corresponding RELION’s post-processed map is presented in Supplementary Figs. 9,10. e, f Atomic model of the core of the RE-RE Hermes transpososome inside its cryo-EM map. f Left: the parallel RE-DNAs inside the complex (only the silhouette of the atomic surface of the Hermes dimers is shown). The features of the DNAs (TIR and STRs) are highlighted. Right: the atomic surface of the Hermes dimers is displayed, while the LE-DNA 1 is shown in cartoon mode.

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