Fig. 5: Dynamic coupling of the RecA2 and Arch domains is mediated by key hydrophobic and salt-bridge interactions. | Nature Communications

Fig. 5: Dynamic coupling of the RecA2 and Arch domains is mediated by key hydrophobic and salt-bridge interactions.

From: Translocation mechanism of xeroderma pigmentosum group D protein on single-stranded DNA and genetic disease etiology

Fig. 5

a A cluster of hydrophobic residues (highlighted by a circle) is positioned between the spring helix and the Arch domain and is key for allosteric communication from the motor domains to the Arch domain. The XPD spring helix is shown in brown; other domains are colored as follows: RecA1 (gold), RecA2 (blue), Arch (magenta), and Fe–S (green). Helix H5 and the spindle helix are labeled. b Zoomed-in view of the hydrophobic interface with interacting residues from the spring helix and the Arch domain shown as spheres and labeled. Salt-bridge interactions involving residues from helix H5, the spindle helix, and the spring helix in (c) the apo state, and (d) the ATP-bound state of XPD. Salt bridges are represented by black dashed lines.

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