 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 5]](dw5092fig5mag.jpg)
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Figure 5
Conformation of the P-loop. (a) The conformation of the P-loop is stabilized by multiple hydrogen bonds (red dashed lines). The ATP binding pocket is occupied by a sulfate ion. (b) Model of bound ATP based on the Vasa–ATP complex structure. ATP binding is hindered by the P-loop owing to the hydrogen bonds between Thr437, Glu550 and Lys441. (c) The P-loop conformation of hPrp28ΔN is unique, as in the structures of eIF4A with bound sulfate or of the DEAD-box helicase Hera with bound phosphate the hydrogen bond between the Glu of the DEAD motif and the Thr or Ser of the P-loop is broken. |
![[Figure 5]](dw5092fig5.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
