 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 4]](ek5032fig4mag.jpg)
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Figure 4
Movement of RecA2 upon nucleotide binding. (a) Comparison of Prp16 models originating from X-ray diffraction and cryo-EM and Prp22 (in a nucleotide-free state). The different structures are shown as ribbons and are aligned via their RecA1-like domains. The RecA2 domain of Prp16–ADP is shifted towards the RecA1 domain compared with the other structures. (b) All structures are depicted as semi-transparent cartoon models. The RecA1 domain is colored orange, the RecA2 domain marine and the C-terminal part gray. The centers of mass of the RecA-like domains are displayed as spheres and colored accordingly. In order to calculate the centers of mass for the same sets of atoms, the RecA1 and RecA2 domains were superimposed and the centers of mass of these superimposed domains were determined. Prp16 structures derived from a cryo-EM model adopt a more open conformation that is comparable to the distances of Prp22 in a nucleotide-free state (PDB entry 6i3o) and the mammalian ortholog DHX38 of yeast Prp16 (bottom right). |
![[Figure 4]](ek5032fig4.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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