Fig. 4: Changes in persistent residue contacts at the RecA1–RecA2 interface during the ATPase cycle. | Nature Communications

Fig. 4: Changes in persistent residue contacts at the RecA1–RecA2 interface during the ATPase cycle.

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

Fig. 4

A zoomed-in view of the XPD ATPase cleft in states: (a) S1; (b) S4; (c) S5; and (d) S7. Panels on the left show XPD residues that are key to the structural integrity of the motor domains interface. Panels on the right show the same key contacts mapped onto the surfaces of the RecA1 (gold) and RecA2 (blue) domains in ‘open-book’ representation. Color-coding is by interaction type: 1) salt bridge-forming residues are in red and blue, 2) hydrogen bonding residues are in cyan and dark brown, and 3) residues involved in hydrophobic contacts are in purple and green.

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