 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](wd5187fig3mag.jpg)
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Figure 3
Ribbon representation of the C-terminal domains of (a) ChpT and (b) DesK (Trajtenberg et al., 2010  ). DesK binds ATP in the ATP-binding pocket defined by the ATP lid (a loop between strand β3 and helix α5) and the central helix α4, while the γ-phosphate is exposed and can be attacked by the catalytic histidine of the DHp domain. In ChpT the ATP lid is substituted by two additional turns in the N-terminal part of helix α5. There is an additional short α-helix (α4′) between strand β5 and helix α5, which together with helix α5 closes the ATP-binding pocket. |
![[Figure 3]](wd5187fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
