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![[Figure 3]](di5014fig3mag.jpg)
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Figure 3
The crystal structure of WalK in the open state. (a) The symmetric structure of open lpWalK in the absence of nucleotides. The two chains are coloured gold and dark green. (b) Structural similarity of the DHp domain to the inactive chain of smVicK is coloured in grey. The phosphorylatable histidine His391 is shown as sticks. (c) The interface between the DHp and CA domains is indicated by a yellow box in (a). Key residues are shown as sticks, with their hydrogen bonds in yellow dashed lines. Residues from the DHp domain are coloured cyan. (d) The conservation of key residues in the open DHp and CA interface between lpWalK and smVicK. The conserved residues in gold are highlighted and labelled based on lpWalK, and the nonconserved residues in smVicK are indicated in blue in parentheses. His391 is coloured red. |
![[Figure 3]](di5014fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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