journal menu
![[Figure 5]](ud5003fig5mag.jpg)
|
|
Figure 5
Comparison of differently bound ADP molecules. ADP molecules are presented as ball-and-stick models and the magnesium ion and water molecules as spheres. ctPrp2 is depicted as a cartoon representation with highlighted residues as ball-and-stick models. (a) depicts the mFo − DFc electron-density OMIT map for the magnesium ion with the four coordinated waters of CF3 (grey) contoured at 3σ. This OMIT map is representative of all ADP-bound structures. The OMIT maps at the same contour level for the ADP molecules of CF2 (orange) and CF3 are displayed in (b) and (c), respectively. (d) On superposing the RecA1 domains of CF2 and CF3 the phosphate moieties align almost identically, but the adenosine is present in a previously undescribed conformation, leading to different adenosine interactions in CF2. (e) A superposition of the different ADP molecules via the ribose reveals that the adenine is present in a syn (CF2) and an anti (CF3) conformation and that the torsions along the C4′—C5′ bond and the C5′—O5′ bond are changed by 167 and 62°, respectively. (f) Depending on the ADP conformations described in (d) and (e), a loop in the nearby motif VI adopts distinct conformations. A superposition of the RecA2 domains reveals a flipped conformation of this loop in the NT-free and CF2 structures compared with CF1 and CF3, which exhibit an ADP-binding pattern comparable to other DExD/H-box helicases. |
![[Figure 5]](ud5003fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
