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![[Figure 1]](di5014fig1mag.jpg)
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Figure 1
The crystal structure of WalK in the closed state. (a) The asymmetrical structure of closed lpWalK bound by the ATP analogue AMPPCP shown as sticks and spheres. The closed monomer is coloured purple and the open monomer is coloured green. (b) The interface between the CA and DHp domains of the open monomer is indicated by a yellow box in (a). Key interacting residues from the DHp domain are shown as cyan sticks and those from the CA domain are shown as green sticks. (c) The interface between the CA and DHp domains of the closed monomer is indicated by a blue box in (a). Key interacting residues from the DHp domain are shown as cyan sticks and those from the CA domain are shown in purple. Hydrogen bonds are highlighted by yellow dashed lines. (d) The conservation of key residues in the closed DHp and CA interface between lpWalK and smVicK. The conserved residues in purple are highlighted and labelled based on lpWalK, and the nonconserved residues in smVicK are indicated in yellow in parentheses. His391 is coloured red. |
![[Figure 1]](di5014fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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