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![[Figure 1]](ud5019fig1mag.jpg)
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Figure 1
Structural overview of the pre-catalytic state of Prp2. (a) Prp2 and the bound RNA are displayed as a cartoon model and ADP-BeF3− is depicted as sticks. The crystallized construct is composed of two RecA-like domains (RecA1, orange; RecA2, blue), a winged-helix (WH) domain (gray), a helix-bundle (HB) domain (wheat) and a oligosaccharide-binding (OB) domain (green). The RNA is bound between the helicase core and the C-terminal domains and the nucleotide is sandwiched between the RecA-like domains. Conserved residues interacting with the RNA backbone of the 3′ stacked region are shown in circles, whereas the remaining interacting residues are shown in rectangular shapes. (b) Superposition of active-site residues of Prp2 and Prp43 interacting with ADP-BeF3− (pale green and blue), the magnesium ion (green) and coordinated water molecules (red). Both DEAH-box ATPases interact with the nucleotide in an identical manner. (c) Superposition of all structurally characterized DExH-box ATPases bound to an ATP analog. The conformation of the helicase core in the ATP-bound state is highly conserved. |
![[Figure 1]](ud5019fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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